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Fluorine in PDB 4ht2: Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.

Enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.

All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor., PDB code: 4ht2 was solved by A.Smirnov, E.Manakova, S.Grazulis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.50 / 1.45
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.709, 67.261, 80.689, 81.78, 84.01, 86.48
R / Rfree (%) 15 / 18.8

Other elements in 4ht2:

The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Fluorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Fluorine atom in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. (pdb code 4ht2). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 20 binding sites of Fluorine where determined in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor., PDB code: 4ht2:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 20 in 4ht2

Go back to Fluorine Binding Sites List in 4ht2
Fluorine binding site 1 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:8.5
occ:0.50
 F13 A:V50302 0.0 8.5 0.5
C4 A:V50302 1.3 6.4 0.5
C5 A:V50302 2.0 7.7 0.5
C4 A:V50302 2.3 8.4 0.5
C3 A:V50302 2.3 5.4 0.5
C5 A:V50302 2.4 3.7 0.5
C6 A:V50302 2.5 9.6 0.5
F12 A:V50302 2.5 9.6 0.5
N23 A:V50302 2.8 9.6 0.5
S7 A:V50302 2.8 8.6 0.5
N23 A:V50302 2.9 3.4 0.5
F13 A:V50302 2.9 11.0 0.5
C3 A:V50302 3.0 8.7 0.5
C1 A:V50302 3.2 12.5 0.5
S7 A:V50302 3.2 5.2 0.5
F11 A:V50302 3.3 10.5 0.5
OG1 A:THR199 3.4 6.4 0.5
CE1 A:HIS91 3.4 4.1 1.0
O9 A:V50302 3.4 6.4 0.5
NE2 A:HIS91 3.4 4.0 1.0
O2 A:EDO304 3.4 22.5 0.5
C2 A:V50302 3.4 11.3 0.5
C2 A:EDO304 3.5 19.2 0.5
CG2 A:THR199 3.6 6.2 0.5
C2 A:V50302 3.6 4.8 0.5
C1 A:EDO304 3.7 17.1 0.5
C6 A:V50302 3.7 5.5 0.5
ZN A:ZN301 3.7 5.0 1.0
O2 A:EDO304 3.8 20.7 0.5
F12 A:V50302 3.9 11.5 0.5
O9 A:V50302 4.0 6.0 0.5
O8 A:V50302 4.0 8.7 0.5
O4 A:PEG303 4.0 33.8 1.0
CB A:THR199 4.1 12.0 0.5
ND1 A:HIS91 4.1 5.3 1.0
CD2 A:HIS91 4.2 6.0 1.0
C1 A:V50302 4.2 9.7 0.5
OG1 A:THR199 4.2 12.3 0.5
O1 A:EDO304 4.2 12.2 0.5
CG2 A:THR199 4.2 6.9 0.5
O8 A:V50302 4.2 3.6 0.5
CB A:THR199 4.2 7.6 0.5
C2 A:EDO304 4.3 15.4 0.5
F10 A:V50302 4.3 12.1 0.5
C1 A:EDO304 4.5 9.7 0.5
CG A:HIS91 4.6 4.8 1.0
O1 A:EDO304 4.6 11.9 0.5
NE2 A:HIS93 4.8 5.0 1.0
F11 A:V50302 4.8 6.6 0.5
CE1 A:HIS93 4.9 5.6 1.0
S14 A:V50302 5.0 11.3 0.5

Fluorine binding site 2 out of 20 in 4ht2

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Fluorine binding site 2 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:11.0
occ:0.50
 F13 A:V50302 0.0 11.0 0.5
C4 A:V50302 1.3 8.4 0.5
C3 A:V50302 1.7 5.4 0.5
C4 A:V50302 1.9 6.4 0.5
C2 A:V50302 1.9 4.8 0.5
C5 A:V50302 2.0 3.7 0.5
C6 A:V50302 2.1 5.5 0.5
C1 A:V50302 2.1 9.7 0.5
C3 A:V50302 2.3 8.7 0.5
C5 A:V50302 2.4 7.7 0.5
F12 A:V50302 2.6 11.5 0.5
F12 A:V50302 2.7 9.6 0.5
O9 A:V50302 2.8 6.4 0.5
CG2 A:VAL119 2.9 7.1 1.0
F13 A:V50302 2.9 8.5 0.5
CE1 A:HIS91 3.1 4.1 1.0
S7 A:V50302 3.2 8.6 0.5
F10 A:V50302 3.2 8.3 0.5
S14 A:V50302 3.3 11.2 0.5
F11 A:V50302 3.3 6.6 0.5
O9 A:V50302 3.4 6.0 0.5
S7 A:V50302 3.4 5.2 0.5
C6 A:V50302 3.6 9.6 0.5
C2 A:V50302 3.6 11.3 0.5
ND1 A:HIS91 3.8 5.3 1.0
NE2 A:GLN89 3.8 14.2 1.0
C1 A:V50302 4.0 12.5 0.5
CB A:VAL119 4.0 5.8 1.0
CG1 A:VAL119 4.1 8.2 1.0
NE2 A:HIS91 4.1 4.0 1.0
CD A:GLN89 4.2 7.3 1.0
N23 A:V50302 4.2 3.4 0.5
N23 A:V50302 4.3 9.6 0.5
O8 A:V50302 4.3 8.7 0.5
OE1 A:GLN89 4.4 8.5 1.0
O8 A:V50302 4.5 3.6 0.5
C15 A:V50302 4.6 9.0 0.5
F11 A:V50302 4.7 10.5 0.5
CD2 A:LEU197 4.7 6.5 0.5
N20 A:V50302 4.8 14.7 0.5
ZN A:ZN301 4.9 5.0 1.0
O1 A:EDO304 4.9 12.2 0.5
N20 A:V50302 4.9 8.6 0.5
CG A:HIS91 5.0 4.8 1.0

Fluorine binding site 3 out of 20 in 4ht2

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Fluorine binding site 3 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:6.6
occ:0.50
 F11 A:V50302 0.0 6.6 0.5
C6 A:V50302 1.4 5.5 0.5
C1 A:V50302 2.4 9.7 0.5
C5 A:V50302 2.4 3.7 0.5
CD2 A:LEU197 2.4 6.5 0.5
F10 A:V50302 2.7 8.3 0.5
O8 A:V50302 2.8 3.6 0.5
S7 A:V50302 2.9 5.2 0.5
O8 A:V50302 2.9 8.7 0.5
O9 A:V50302 2.9 6.4 0.5
C5 A:V50302 3.0 7.7 0.5
O9 A:V50302 3.0 6.0 0.5
S7 A:V50302 3.0 8.6 0.5
C4 A:V50302 3.2 8.4 0.5
F13 A:V50302 3.3 11.0 0.5
CG2 A:VAL141 3.3 7.0 1.0
CG A:LEU197 3.5 7.2 0.5
CD1 A:LEU197 3.6 12.3 0.5
C2 A:V50302 3.6 4.8 0.5
C4 A:V50302 3.7 6.4 0.5
C6 A:V50302 3.7 9.6 0.5
CG A:LEU197 3.9 6.5 0.5
C3 A:V50302 4.1 8.7 0.5
C3 A:V50302 4.1 5.4 0.5
CG2 A:VAL119 4.2 7.1 1.0
CG2 A:VAL206 4.2 7.8 1.0
CG1 A:VAL119 4.3 8.2 1.0
F11 A:V50302 4.4 10.5 0.5
N23 A:V50302 4.4 3.4 0.5
CA A:LEU197 4.5 5.8 0.5
CA A:LEU197 4.5 5.6 0.5
CB A:LEU197 4.5 6.8 0.5
CD2 A:LEU197 4.5 11.8 0.5
C1 A:V50302 4.5 12.5 0.5
CB A:LEU197 4.5 7.0 0.5
CB A:VAL141 4.6 5.5 1.0
N23 A:V50302 4.6 9.6 0.5
C2 A:V50302 4.7 11.3 0.5
CD1 A:LEU139 4.7 10.7 1.0
CG1 A:VAL141 4.8 7.0 1.0
F13 A:V50302 4.8 8.5 0.5
F12 A:V50302 4.8 11.5 0.5
CB A:VAL119 4.9 5.8 1.0
CD1 A:LEU197 5.0 9.7 0.5

Fluorine binding site 4 out of 20 in 4ht2

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Fluorine binding site 4 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:10.5
occ:0.50
 F11 A:V50302 0.0 10.5 0.5
C6 A:V50302 1.3 9.6 0.5
OG1 A:THR199 2.1 6.4 0.5
C1 A:V50302 2.3 12.5 0.5
C5 A:V50302 2.4 7.7 0.5
F10 A:V50302 2.6 12.1 0.5
N A:THR199 2.7 5.0 0.5
N A:THR199 2.8 6.8 0.5
O8 A:V50302 2.8 8.7 0.5
CB A:THR199 2.9 12.0 0.5
O8 A:V50302 2.9 3.6 0.5
C5 A:V50302 3.0 3.7 0.5
CB A:LEU197 3.0 7.0 0.5
CG A:LEU197 3.0 7.2 0.5
S7 A:V50302 3.0 8.6 0.5
N A:THR198 3.1 5.0 1.0
CB A:THR199 3.1 7.6 0.5
CB A:LEU197 3.1 6.8 0.5
C4 A:V50302 3.2 6.4 0.5
CD2 A:LEU197 3.2 11.8 0.5
N23 A:V50302 3.2 9.6 0.5
N23 A:V50302 3.2 3.4 0.5
S7 A:V50302 3.2 5.2 0.5
O A:THR199 3.2 5.7 0.5
F13 A:V50302 3.3 8.5 0.5
CG2 A:THR199 3.3 6.9 0.5
CG2 A:THR199 3.3 6.2 0.5
CA A:THR199 3.3 5.3 0.5
CA A:THR199 3.4 7.1 0.5
C A:LEU197 3.5 5.6 0.5
CA A:LEU197 3.5 5.8 0.5
CA A:LEU197 3.5 5.6 0.5
C4 A:V50302 3.6 8.4 0.5
C A:LEU197 3.6 5.2 0.5
C2 A:V50302 3.6 11.3 0.5
O A:THR199 3.6 5.8 0.5
C A:THR198 3.7 6.0 1.0
C A:THR199 3.7 7.0 0.5
C6 A:V50302 3.8 5.5 0.5
OG1 A:THR199 3.8 12.3 0.5
C A:THR199 3.8 6.0 0.5
CD2 A:LEU197 3.9 6.5 0.5
CA A:THR198 3.9 4.2 1.0
CG A:LEU197 4.0 6.5 0.5
OG1 A:THR198 4.0 5.0 1.0
C3 A:V50302 4.0 8.7 0.5
C3 A:V50302 4.1 5.4 0.5
O9 A:V50302 4.3 6.4 0.5
O A:LEU197 4.4 5.6 0.5
F11 A:V50302 4.4 6.6 0.5
CD1 A:LEU197 4.4 12.3 0.5
O A:LEU197 4.6 4.8 0.5
C1 A:V50302 4.6 9.7 0.5
CB A:THR198 4.6 5.1 1.0
CD1 A:LEU197 4.7 9.7 0.5
O9 A:V50302 4.7 6.0 0.5
F13 A:V50302 4.7 11.0 0.5
C2 A:V50302 4.7 4.8 0.5
F12 A:V50302 4.8 9.6 0.5
O A:THR198 4.8 5.4 1.0
O4 A:PEG303 4.9 33.8 1.0
O A:PRO200 4.9 9.6 1.0
N A:LEU197 5.0 5.6 0.5
N A:LEU197 5.0 5.7 0.5

Fluorine binding site 5 out of 20 in 4ht2

Go back to Fluorine Binding Sites List in 4ht2
Fluorine binding site 5 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:8.3
occ:0.50
 F10 A:V50302 0.0 8.3 0.5
C1 A:V50302 1.3 9.7 0.5
C2 A:V50302 2.4 4.8 0.5
C6 A:V50302 2.4 5.5 0.5
C21 A:V50302 2.6 18.7 0.5
F11 A:V50302 2.7 6.6 0.5
N20 A:V50302 2.9 14.7 0.5
S14 A:V50302 3.0 11.2 0.5
CD2 A:LEU197 3.1 6.5 0.5
CG1 A:VAL119 3.1 8.2 1.0
N20 A:V50302 3.2 8.6 0.5
C15 A:V50302 3.2 9.0 0.5
C4 A:V50302 3.2 8.4 0.5
C3 A:V50302 3.2 8.7 0.5
F13 A:V50302 3.2 11.0 0.5
C19 A:V50302 3.3 17.6 0.5
F12 A:V50302 3.3 11.5 0.5
C3 A:V50302 3.6 5.4 0.5
C5 A:V50302 3.7 3.7 0.5
CD1 A:LEU139 3.8 10.7 1.0
C2 A:V50302 3.9 11.3 0.5
CD1 A:LEU197 3.9 12.3 0.5
C5 A:V50302 4.0 7.7 0.5
N16 A:V50302 4.1 13.5 0.5
C19 A:V50302 4.2 12.4 0.5
C4 A:V50302 4.2 6.4 0.5
C15 A:V50302 4.2 12.9 0.5
CG A:LEU197 4.2 7.2 0.5
CG2 A:VAL119 4.2 7.1 1.0
CB A:VAL119 4.3 5.8 1.0
CD2 A:LEU197 4.4 11.8 0.5
CG A:LEU197 4.4 6.5 0.5
C1 A:V50302 4.5 12.5 0.5
C6 A:V50302 4.5 9.6 0.5
CD2 A:LEU139 4.6 12.4 1.0
C18 A:V50302 4.6 19.4 0.5
CD1 A:LEU197 4.7 9.7 0.5
F12 A:V50302 4.7 9.6 0.5
CG A:LEU139 4.7 7.9 1.0
C21 A:V50302 4.8 11.6 0.5
O9 A:V50302 4.8 6.4 0.5
S14 A:V50302 4.8 11.3 0.5
C17 A:V50302 4.9 8.6 0.5
C18 A:V50302 5.0 11.7 0.5

Fluorine binding site 6 out of 20 in 4ht2

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Fluorine binding site 6 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:12.1
occ:0.50
 F10 A:V50302 0.0 12.1 0.5
C1 A:V50302 1.4 12.5 0.5
CD2 A:LEU197 2.1 11.8 0.5
OG1 A:THR199 2.2 6.4 0.5
C2 A:V50302 2.4 11.3 0.5
C6 A:V50302 2.4 9.6 0.5
F11 A:V50302 2.6 10.5 0.5
O A:THR199 2.7 5.7 0.5
CG2 A:THR199 2.8 6.9 0.5
O A:PRO200 2.9 9.6 1.0
S14 A:V50302 3.0 11.3 0.5
CG A:LEU197 3.1 7.2 0.5
O A:THR199 3.3 5.8 0.5
CB A:THR199 3.4 7.6 0.5
C A:THR199 3.5 7.0 0.5
C A:PRO200 3.5 8.0 1.0
CB A:THR199 3.5 12.0 0.5
O4 A:PEG303 3.6 33.8 1.0
CB A:LEU197 3.6 7.0 0.5
C3 A:V50302 3.6 8.7 0.5
C A:THR199 3.6 6.0 0.5
CB A:LEU197 3.6 6.8 0.5
CD1 A:LEU197 3.7 9.7 0.5
C5 A:V50302 3.7 7.7 0.5
CD A:PRO201 3.8 8.5 1.0
N A:PRO201 3.9 8.1 1.0
CA A:THR199 3.9 5.3 0.5
CG A:LEU197 3.9 6.5 0.5
C4 A:V50302 4.0 6.4 0.5
C3 A:V50302 4.0 5.4 0.5
CA A:THR199 4.1 7.1 0.5
C4 A:V50302 4.1 8.4 0.5
N A:THR199 4.2 5.0 0.5
C15 A:V50302 4.2 12.9 0.5
N A:THR199 4.2 6.8 0.5
CD2 A:LEU197 4.2 6.5 0.5
F13 A:V50302 4.3 8.5 0.5
CD1 A:LEU197 4.3 12.3 0.5
N A:PRO200 4.3 8.0 1.0
C5 A:V50302 4.3 3.7 0.5
N20 A:V50302 4.4 8.6 0.5
F12 A:V50302 4.4 9.6 0.5
C4 A:PEG303 4.4 26.3 1.0
CG2 A:THR199 4.4 6.2 0.5
C2 A:V50302 4.5 4.8 0.5
CA A:PRO200 4.5 7.1 1.0
C21 A:V50302 4.6 11.6 0.5
N20 A:V50302 4.6 14.7 0.5
N A:CYS202 4.7 7.3 1.0
F12 A:V50302 4.7 11.5 0.5
C1 A:V50302 4.7 9.7 0.5
C6 A:V50302 4.7 5.5 0.5
OG1 A:THR199 4.8 12.3 0.5
CA A:LEU197 4.9 5.8 0.5
CA A:LEU197 4.9 5.6 0.5

Fluorine binding site 7 out of 20 in 4ht2

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Fluorine binding site 7 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:9.6
occ:0.50
 F12 A:V50302 0.0 9.6 0.5
C3 A:V50302 1.3 5.4 0.5
C3 A:V50302 1.7 8.7 0.5
F12 A:V50302 1.9 11.5 0.5
C4 A:V50302 2.3 6.4 0.5
C4 A:V50302 2.3 8.4 0.5
C2 A:V50302 2.4 4.8 0.5
C2 A:V50302 2.5 11.3 0.5
F13 A:V50302 2.5 8.5 0.5
F13 A:V50302 2.7 11.0 0.5
S14 A:V50302 3.0 11.2 0.5
O1 A:EDO304 3.2 12.2 0.5
C1 A:V50302 3.3 12.5 0.5
C5 A:V50302 3.3 7.7 0.5
O4 A:PEG303 3.4 33.8 1.0
NE2 A:GLN89 3.4 14.2 1.0
S14 A:V50302 3.4 11.3 0.5
C1 A:EDO304 3.5 17.1 0.5
C6 A:V50302 3.6 9.6 0.5
C5 A:V50302 3.6 3.7 0.5
O2 A:PEG303 3.6 38.4 1.0
C3 A:PEG303 3.6 27.7 1.0
C1 A:V50302 3.6 9.7 0.5
C2 A:PEG303 3.7 23.3 1.0
C4 A:PEG303 3.8 26.3 1.0
O1 A:EDO304 4.0 11.9 0.5
C6 A:V50302 4.1 5.5 0.5
C2 A:EDO304 4.1 15.4 0.5
C1 A:EDO304 4.1 9.7 0.5
C15 A:V50302 4.2 9.0 0.5
C2 A:EDO304 4.3 19.2 0.5
CE1 A:HIS91 4.4 4.1 1.0
F10 A:V50302 4.4 12.1 0.5
C15 A:V50302 4.4 12.9 0.5
N20 A:V50302 4.5 14.7 0.5
OG1 A:THR199 4.5 6.4 0.5
CD A:GLN89 4.5 7.3 1.0
O2 A:EDO304 4.5 20.7 0.5
N20 A:V50302 4.5 8.6 0.5
ND1 A:HIS91 4.5 5.3 1.0
O2 A:EDO304 4.7 22.5 0.5
O A:HOH632 4.7 27.5 1.0
F10 A:V50302 4.7 8.3 0.5
S7 A:V50302 4.8 8.6 0.5
F11 A:V50302 4.8 10.5 0.5
O9 A:V50302 4.9 6.4 0.5
NE2 A:HIS91 5.0 4.0 1.0

Fluorine binding site 8 out of 20 in 4ht2

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Fluorine binding site 8 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:11.5
occ:0.50
 F12 A:V50302 0.0 11.5 0.5
S14 A:V50302 1.1 11.2 0.5
C2 A:V50302 1.2 4.8 0.5
C3 A:V50302 1.4 8.7 0.5
C3 A:V50302 1.7 5.4 0.5
F12 A:V50302 1.9 9.6 0.5
C2 A:V50302 2.3 11.3 0.5
C4 A:V50302 2.4 8.4 0.5
C15 A:V50302 2.4 9.0 0.5
C1 A:V50302 2.6 9.7 0.5
F13 A:V50302 2.6 11.0 0.5
N20 A:V50302 2.9 14.7 0.5
S14 A:V50302 3.0 11.3 0.5
N20 A:V50302 3.0 8.6 0.5
C4 A:V50302 3.0 6.4 0.5
C15 A:V50302 3.2 12.9 0.5
F10 A:V50302 3.3 8.3 0.5
N16 A:V50302 3.5 13.5 0.5
NE2 A:GLN89 3.5 14.2 1.0
C1 A:V50302 3.6 12.5 0.5
C6 A:V50302 3.6 5.5 0.5
C5 A:V50302 3.7 7.7 0.5
C5 A:V50302 3.8 3.7 0.5
O A:HOH632 3.9 27.5 1.0
C19 A:V50302 3.9 17.6 0.5
F13 A:V50302 3.9 8.5 0.5
C6 A:V50302 4.1 9.6 0.5
O2 A:PEG303 4.1 38.4 1.0
C2 A:PEG303 4.2 23.3 1.0
N16 A:V50302 4.3 17.6 0.5
C19 A:V50302 4.3 12.4 0.5
C21 A:V50302 4.3 18.7 0.5
CD A:GLN89 4.4 7.3 1.0
O1 A:EDO304 4.6 12.2 0.5
O4 A:PEG303 4.6 33.8 1.0
C3 A:PEG303 4.6 27.7 1.0
C17 A:V50302 4.6 8.6 0.5
F10 A:V50302 4.7 12.1 0.5
O A:HOH543 4.7 22.9 1.0
C4 A:PEG303 4.7 26.3 1.0
CG2 A:VAL119 4.8 7.1 1.0
F11 A:V50302 4.8 6.6 0.5
CD2 A:LEU197 4.9 11.8 0.5
CG1 A:VAL119 4.9 8.2 1.0
CG A:GLN89 4.9 7.3 1.0
C18 A:V50302 5.0 19.4 0.5

Fluorine binding site 9 out of 20 in 4ht2

Go back to Fluorine Binding Sites List in 4ht2
Fluorine binding site 9 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F302

b:10.2
occ:1.00
 F13 B:V50302 0.0 10.2 1.0
C4 B:V50302 1.3 8.8 1.0
C3 B:V50302 2.3 7.5 1.0
C5 B:V50302 2.4 7.2 1.0
F12 B:V50302 2.7 10.3 1.0
O8 B:V50302 2.8 7.8 1.0
N B:THR199 2.8 6.9 1.0
N B:THR198 2.9 6.2 1.0
S7 B:V50302 2.9 7.9 1.0
N23 B:V50302 3.2 7.9 1.0
OG1 B:THR199 3.2 10.1 1.0
CB B:LEU197 3.3 6.3 1.0
CA B:LEU197 3.5 6.6 1.0
C B:LEU197 3.5 6.0 1.0
C2 B:V50302 3.6 9.3 1.0
C6 B:V50302 3.6 8.0 1.0
C B:THR198 3.7 7.0 1.0
CA B:THR199 3.7 7.2 1.0
O B:THR199 3.7 6.6 1.0
CG2 B:THR199 3.7 8.0 1.0
CB B:THR199 3.7 8.7 1.0
CA B:THR198 3.7 5.4 1.0
OG1 B:THR198 3.8 5.1 1.0
CD2 B:LEU197 3.9 9.0 1.0
C1 B:V50302 4.0 9.3 1.0
C B:THR199 4.1 6.6 1.0
CG B:LEU197 4.1 7.1 1.0
O9 B:V50302 4.3 8.0 1.0
CB B:THR198 4.4 4.7 1.0
O B:LEU197 4.4 5.4 1.0
F11 B:V50302 4.7 11.0 1.0
CD1 B:LEU197 4.7 11.1 1.0
O B:THR198 4.8 6.3 1.0
C2 B:EDO304 4.9 15.7 1.0
N B:LEU197 5.0 6.0 1.0

Fluorine binding site 10 out of 20 in 4ht2

Go back to Fluorine Binding Sites List in 4ht2
Fluorine binding site 10 out of 20 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of Crystal Structure of Human Carbonic Anhydrase Isozyme XII with the Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F302

b:11.0
occ:1.00
 F11 B:V50302 0.0 11.0 1.0
C6 B:V50302 1.3 8.0 1.0
C5 B:V50302 2.3 7.2 1.0
C1 B:V50302 2.4 9.3 1.0
F10 B:V50302 2.6 11.7 1.0
O9 B:V50302 2.8 8.0 1.0
CE1 B:HIS91 3.0 5.7 1.0
CG2 B:VAL119 3.2 7.1 1.0
S7 B:V50302 3.2 7.9 1.0
OE1 B:GLN89 3.5 14.4 1.0
C2 B:EDO304 3.6 15.7 1.0
C4 B:V50302 3.6 8.8 1.0
C2 B:V50302 3.6 9.3 1.0
ND1 B:HIS91 3.7 5.8 1.0
O2 B:EDO304 3.8 18.8 1.0
NE2 B:HIS91 4.0 5.0 1.0
CD B:GLN89 4.1 8.4 1.0
C3 B:V50302 4.1 7.5 1.0
CG1 B:VAL119 4.1 7.9 1.0
N23 B:V50302 4.2 7.9 1.0
CB B:VAL119 4.2 6.5 1.0
O8 B:V50302 4.3 7.8 1.0
NE2 B:GLN89 4.4 6.3 1.0
N20 B:V50302 4.7 9.7 1.0
F13 B:V50302 4.7 10.2 1.0
ZN B:ZN301 4.8 5.8 1.0
C1 B:EDO304 4.8 19.6 1.0
CG B:HIS91 4.9 5.9 1.0
CD2 B:LEU197 4.9 9.0 1.0
CD2 B:HIS91 5.0 9.1 1.0

Reference:

V.Dudutiene, A.Zubriene, A.Smirnov, J.Gylyte, D.Timm, E.Manakova, S.Grazulis, D.Matulis. 4-Substituted-2,3,5,6-Tetrafluorobenzenesulfonamides As Inhibitors of Carbonic Anhydrases I, II, VII, XII, and XIII. Bioorg.Med.Chem. V. 21 2093 2013.
ISSN: ISSN 0968-0896
PubMed: 23394791
DOI: 10.1016/J.BMC.2013.01.008
Page generated: Thu Aug 1 02:07:58 2024

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