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Fluorine in PDB 4qjo: Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor

Enzymatic activity of Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor

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

Protein crystallography data

The structure of Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor, PDB code: 4qjo 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) 23.59 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.498, 66.558, 80.318, 81.98, 84.31, 86.45
R / Rfree (%) 16.1 / 20.6

Other elements in 4qjo:

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

Zinc (Zn) 4 atoms

Fluorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Fluorine atom in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor (pdb code 4qjo). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 12 binding sites of Fluorine where determined in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor, PDB code: 4qjo:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 12 in 4qjo

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Fluorine binding site 1 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F303

b:38.3
occ:1.00
 F26 A:V1F303 0.0 38.3 1.0
C5 A:V1F303 1.4 35.1 1.0
C4 A:V1F303 2.4 28.3 1.0
C6 A:V1F303 2.4 38.5 1.0
C14 A:V1F303 2.7 46.1 1.0
N25 A:V1F303 2.9 40.3 1.0
S7 A:V1F303 3.0 19.7 1.0
O8 A:V1F303 3.0 18.5 1.0
CD2 A:LEU197 3.1 14.6 1.0
O9 A:V1F303 3.3 18.6 1.0
C3 A:V1F303 3.7 32.7 1.0
C1 A:V1F303 3.7 47.5 1.0
CG2 A:VAL119 3.8 11.8 1.0
CG1 A:VAL119 4.1 11.3 1.0
C15 A:V1F303 4.1 54.8 1.0
C2 A:V1F303 4.2 44.7 1.0
CG A:LEU197 4.3 12.4 1.0
CE1 A:HIS91 4.5 9.3 1.0
CB A:VAL119 4.6 11.2 1.0
N10 A:V1F303 4.7 16.2 1.0
CD1 A:LEU197 4.8 16.3 1.0
CB A:LEU197 4.8 11.1 1.0
F12 A:V1F303 4.8 34.7 1.0
CG2 A:VAL141 4.8 9.5 1.0
C20 A:V1F303 4.9 59.5 1.0
C16 A:V1F303 5.0 55.1 1.0
C32 A:V1F303 5.0 59.3 1.0

Fluorine binding site 2 out of 12 in 4qjo

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Fluorine binding site 2 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F303

b:34.7
occ:1.00
 F12 A:V1F303 0.0 34.7 1.0
C3 A:V1F303 1.4 32.7 1.0
C2 A:V1F303 2.4 44.7 1.0
C4 A:V1F303 2.4 28.3 1.0
ZN A:ZN302 2.7 10.8 1.0
F13 A:V1F303 2.7 47.1 1.0
N10 A:V1F303 2.8 16.2 1.0
NE2 A:HIS91 3.0 8.2 1.0
CG2 A:THR199 3.0 10.8 1.0
S7 A:V1F303 3.0 19.7 1.0
CE1 A:HIS93 3.3 8.2 1.0
NE2 A:HIS93 3.4 8.2 1.0
CE1 A:HIS91 3.6 9.3 1.0
C1 A:V1F303 3.7 47.5 1.0
C5 A:V1F303 3.7 35.1 1.0
CD2 A:HIS91 3.7 8.3 1.0
OG1 A:THR198 4.0 7.9 1.0
OG1 A:THR199 4.0 14.6 1.0
O9 A:V1F303 4.1 18.6 1.0
CB A:THR199 4.1 10.6 1.0
C6 A:V1F303 4.2 38.5 1.0
O8 A:V1F303 4.3 18.5 1.0
O A:HOH438 4.4 23.3 1.0
ND1 A:HIS91 4.5 8.9 1.0
ND1 A:HIS93 4.6 9.3 1.0
CG A:HIS91 4.6 9.3 1.0
CD2 A:HIS93 4.7 8.1 1.0
N A:THR199 4.7 8.3 1.0
ND1 A:HIS117 4.8 8.4 1.0
F26 A:V1F303 4.8 38.3 1.0
O A:HOH410 5.0 12.2 1.0

Fluorine binding site 3 out of 12 in 4qjo

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Fluorine binding site 3 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F303

b:47.1
occ:1.00
 F13 A:V1F303 0.0 47.1 1.0
C2 A:V1F303 1.4 44.7 1.0
C3 A:V1F303 2.4 32.7 1.0
C1 A:V1F303 2.4 47.5 1.0
F12 A:V1F303 2.7 34.7 1.0
S11 A:V1F303 3.0 61.3 1.0
O23 A:V1F303 3.1 64.8 1.0
C4 A:V1F303 3.7 28.3 1.0
C21 A:V1F303 3.7 57.5 1.0
C6 A:V1F303 3.7 38.5 1.0
CG2 A:THR199 3.7 10.8 1.0
OG1 A:THR199 3.9 14.6 1.0
O A:HOH438 4.0 23.3 1.0
C24 A:V1F303 4.0 58.0 1.0
C5 A:V1F303 4.2 35.1 1.0
CB A:THR199 4.3 10.6 1.0
NE2 A:HIS91 4.3 8.2 1.0
CD2 A:HIS91 4.4 8.3 1.0
O22 A:V1F303 4.4 60.5 1.0
CE1 A:HIS91 4.5 9.3 1.0
ND2 A:ASN64 4.6 26.5 1.0
CG A:HIS91 4.7 9.3 1.0
ND1 A:HIS91 4.8 8.9 1.0
CB A:SER67 4.8 17.1 1.0
N25 A:V1F303 4.8 40.3 1.0

Fluorine binding site 4 out of 12 in 4qjo

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Fluorine binding site 4 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F304

b:34.4
occ:1.00
 F26 B:V1F304 0.0 34.4 1.0
C5 B:V1F304 1.3 27.5 1.0
C4 B:V1F304 2.3 24.4 1.0
C6 B:V1F304 2.4 33.7 1.0
O9 B:V1F304 2.7 14.7 1.0
N25 B:V1F304 2.7 32.5 1.0
CE1 B:HIS91 2.9 11.6 1.0
CG2 B:VAL119 3.0 11.7 1.0
C14 B:V1F304 3.1 35.8 1.0
S7 B:V1F304 3.1 17.9 1.0
C3 B:V1F304 3.6 31.6 1.0
C1 B:V1F304 3.7 37.6 1.0
ND1 B:HIS91 3.7 10.6 1.0
NE2 B:HIS91 3.8 11.2 1.0
NE2 B:GLN89 4.0 14.8 1.0
OE1 B:GLN89 4.1 24.0 1.0
C2 B:V1F304 4.1 37.1 1.0
O8 B:V1F304 4.1 14.7 1.0
CB B:VAL119 4.1 10.4 1.0
CG1 B:VAL119 4.2 10.6 1.0
CD B:GLN89 4.2 17.1 1.0
N10 B:V1F304 4.2 17.8 1.0
C31 B:V1F304 4.3 32.0 1.0
C32 B:V1F304 4.4 33.5 1.0
C15 B:V1F304 4.5 36.5 1.0
C27 B:V1F304 4.6 33.7 1.0
ZN B:ZN303 4.6 10.1 1.0
F12 B:V1F304 4.7 33.7 1.0
C30 B:V1F304 4.8 35.1 1.0
CG B:HIS91 4.8 10.7 1.0
CD2 B:HIS91 4.9 10.8 1.0
CD2 B:LEU197 4.9 10.1 1.0
C28 B:V1F304 4.9 32.4 1.0

Fluorine binding site 5 out of 12 in 4qjo

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Fluorine binding site 5 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F304

b:33.7
occ:1.00
 F12 B:V1F304 0.0 33.7 1.0
C3 B:V1F304 1.4 31.6 1.0
C4 B:V1F304 2.4 24.4 1.0
C2 B:V1F304 2.4 37.1 1.0
O8 B:V1F304 2.7 14.7 1.0
N B:THR199 2.7 9.9 1.0
N B:THR198 2.7 9.4 1.0
F13 B:V1F304 2.8 45.3 1.0
S7 B:V1F304 2.9 17.9 1.0
OG1 B:THR199 2.9 16.2 1.0
CB B:LEU197 3.2 9.5 1.0
C B:LEU197 3.4 8.4 1.0
CA B:LEU197 3.4 9.7 1.0
N10 B:V1F304 3.4 17.8 1.0
C B:THR198 3.5 9.8 1.0
CA B:THR199 3.6 11.0 1.0
CB B:THR199 3.6 12.6 1.0
C5 B:V1F304 3.6 27.5 1.0
C1 B:V1F304 3.7 37.6 1.0
CA B:THR198 3.7 8.5 1.0
OG1 B:THR198 3.7 7.8 1.0
CG2 B:THR199 3.7 13.1 1.0
O B:THR199 3.7 12.3 1.0
CD2 B:LEU197 3.9 10.1 1.0
CG B:LEU197 4.0 10.4 1.0
C B:THR199 4.1 11.0 1.0
C6 B:V1F304 4.1 33.7 1.0
CB B:THR198 4.3 8.5 1.0
O B:LEU197 4.4 9.8 1.0
O9 B:V1F304 4.4 14.7 1.0
O B:THR198 4.6 8.6 1.0
CD1 B:LEU197 4.7 10.2 1.0
F26 B:V1F304 4.7 34.4 1.0
C28 B:V1F304 4.7 32.4 1.0
N B:LEU197 4.8 9.7 1.0

Fluorine binding site 6 out of 12 in 4qjo

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Fluorine binding site 6 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F304

b:45.3
occ:1.00
 F13 B:V1F304 0.0 45.3 1.0
C2 B:V1F304 1.4 37.1 1.0
OG1 B:THR199 2.3 16.2 1.0
C1 B:V1F304 2.3 37.6 1.0
C3 B:V1F304 2.4 31.6 1.0
O22 B:V1F304 2.7 43.6 1.0
F12 B:V1F304 2.8 33.7 1.0
S11 B:V1F304 2.9 45.2 1.0
O B:PRO200 3.1 12.2 1.0
O23 B:V1F304 3.2 40.4 1.0
O B:THR199 3.2 12.3 1.0
CD1 B:LEU197 3.5 10.2 1.0
CB B:THR199 3.6 12.6 1.0
C6 B:V1F304 3.6 33.7 1.0
CB B:LEU197 3.7 9.5 1.0
C B:THR199 3.7 11.0 1.0
C4 B:V1F304 3.7 24.4 1.0
C B:PRO200 3.7 10.4 1.0
C29 B:V1F304 3.9 40.7 1.0
CG B:LEU197 3.9 10.4 1.0
CD B:PRO201 4.0 10.2 1.0
CA B:THR199 4.0 11.0 1.0
N B:THR199 4.1 9.9 1.0
N B:PRO201 4.1 10.2 1.0
C5 B:V1F304 4.2 27.5 1.0
CD2 B:LEU197 4.2 10.1 1.0
C28 B:V1F304 4.4 32.4 1.0
N B:PRO200 4.5 10.5 1.0
CG2 B:THR199 4.5 13.1 1.0
C21 B:V1F304 4.6 44.2 1.0
C30 B:V1F304 4.7 35.1 1.0
CA B:PRO200 4.8 10.6 1.0
N25 B:V1F304 4.8 32.5 1.0
CA B:LEU197 4.8 9.7 1.0
N B:CYS202 4.9 9.2 1.0
C24 B:V1F304 5.0 44.6 1.0

Fluorine binding site 7 out of 12 in 4qjo

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Fluorine binding site 7 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F302

b:36.5
occ:1.00
 F26 C:V1F302 0.0 36.5 1.0
C5 C:V1F302 1.3 32.4 1.0
C4 C:V1F302 2.3 30.9 1.0
C6 C:V1F302 2.4 39.9 1.0
C14 C:V1F302 2.4 40.2 1.0
N25 C:V1F302 2.8 38.8 1.0
S7 C:V1F302 3.0 21.7 1.0
O9 C:V1F302 3.0 18.2 1.0
CD2 C:LEU197 3.0 18.2 1.0
O8 C:V1F302 3.5 19.2 1.0
C3 C:V1F302 3.6 31.8 1.0
CG2 C:VAL119 3.6 8.9 1.0
C1 C:V1F302 3.7 46.5 1.0
C15 C:V1F302 3.9 46.0 1.0
CG1 C:VAL119 4.0 8.2 1.0
C2 C:V1F302 4.2 42.8 1.0
CG C:LEU197 4.4 16.9 1.0
CB C:VAL119 4.4 8.6 1.0
CE1 C:HIS91 4.4 10.5 1.0
C20 C:V1F302 4.5 45.0 1.0
N10 C:V1F302 4.6 16.9 1.0
F12 C:V1F302 4.6 38.7 1.0
CD1 C:LEU197 4.7 20.6 1.0
CG2 C:VAL141 4.8 9.4 1.0
C16 C:V1F302 4.9 48.8 1.0
CB C:LEU197 5.0 14.2 1.0

Fluorine binding site 8 out of 12 in 4qjo

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Fluorine binding site 8 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F302

b:38.7
occ:1.00
 F12 C:V1F302 0.0 38.7 1.0
C3 C:V1F302 1.3 31.8 1.0
N10 C:V1F302 2.0 16.9 1.0
C4 C:V1F302 2.3 30.9 1.0
C2 C:V1F302 2.4 42.8 1.0
ZN C:ZN301 2.6 9.8 1.0
F13 C:V1F302 2.8 46.5 1.0
S7 C:V1F302 2.9 21.7 1.0
NE2 C:HIS91 3.0 9.9 1.0
CE1 C:HIS93 3.3 8.4 1.0
NE2 C:HIS93 3.3 8.5 1.0
CG2 C:THR199 3.4 11.3 1.0
C5 C:V1F302 3.6 32.4 1.0
OG1 C:THR198 3.6 7.6 1.0
CE1 C:HIS91 3.7 10.5 1.0
C1 C:V1F302 3.7 46.5 1.0
CD2 C:HIS91 3.8 10.8 1.0
OG1 C:THR199 3.9 13.6 1.0
O8 C:V1F302 3.9 19.2 1.0
O9 C:V1F302 3.9 18.2 1.0
C6 C:V1F302 4.1 39.9 1.0
CB C:THR199 4.2 10.7 1.0
N C:THR199 4.5 9.0 1.0
O C:HOH446 4.6 18.4 1.0
ND1 C:HIS91 4.6 11.1 1.0
F26 C:V1F302 4.6 36.5 1.0
ND1 C:HIS117 4.6 8.0 1.0
ND1 C:HIS93 4.6 9.2 1.0
CD2 C:HIS93 4.7 8.5 1.0
CG C:HIS91 4.7 10.1 1.0
O C:HOH421 4.8 10.3 1.0
C C:THR198 4.9 8.6 1.0
N C:THR198 5.0 8.5 1.0
CB C:THR198 5.0 8.4 1.0
CA C:THR199 5.0 9.8 1.0

Fluorine binding site 9 out of 12 in 4qjo

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Fluorine binding site 9 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F302

b:46.5
occ:1.00
 F13 C:V1F302 0.0 46.5 1.0
C2 C:V1F302 1.4 42.8 1.0
C3 C:V1F302 2.4 31.8 1.0
C1 C:V1F302 2.5 46.5 1.0
O23 C:V1F302 2.7 56.5 1.0
F12 C:V1F302 2.8 38.7 1.0
O C:HOH578 3.1 38.8 1.0
S11 C:V1F302 3.1 59.7 1.0
CG2 C:THR199 3.5 11.3 1.0
OG1 C:THR199 3.6 13.6 1.0
C4 C:V1F302 3.7 30.9 1.0
C6 C:V1F302 3.7 39.9 1.0
O C:HOH446 3.8 18.4 1.0
O22 C:V1F302 4.0 62.3 1.0
CB C:THR199 4.1 10.7 1.0
C5 C:V1F302 4.2 32.4 1.0
NE2 C:HIS91 4.5 9.9 1.0
CD2 C:HIS91 4.6 10.8 1.0
CE1 C:HIS91 4.7 10.5 1.0
C21 C:V1F302 4.7 59.9 1.0
C24 C:V1F302 4.8 55.9 1.0
N10 C:V1F302 4.9 16.9 1.0
CG C:HIS91 4.9 10.1 1.0
CB C:SER67 4.9 17.0 1.0
CE1 C:HIS93 4.9 8.4 1.0
ND1 C:HIS91 4.9 11.1 1.0
N25 C:V1F302 5.0 38.8 1.0

Fluorine binding site 10 out of 12 in 4qjo

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Fluorine binding site 10 out of 12 in the Crystal Structure of Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with 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 Catalytic Domain of Human Carbonic Anhydrase Isozyme XII with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
D:F302

b:52.3
occ:1.00
 F26 D:V1F302 0.0 52.3 1.0
C5 D:V1F302 1.3 40.9 1.0
C4 D:V1F302 2.3 32.4 1.0
C6 D:V1F302 2.4 46.1 1.0
CE1 D:HIS91 2.6 12.9 1.0
N25 D:V1F302 2.8 52.8 1.0
O9 D:V1F302 2.8 17.2 1.0
CG2 D:VAL119 2.9 13.2 1.0
C14 D:V1F302 2.9 50.1 1.0
S7 D:V1F302 3.1 20.4 1.0
ND1 D:HIS91 3.4 12.1 1.0
C3 D:V1F302 3.6 43.3 1.0
NE2 D:HIS91 3.6 13.5 1.0
OE1 D:GLN89 3.7 25.8 1.0
C1 D:V1F302 3.7 54.0 1.0
CD D:GLN89 4.0 18.3 1.0
C2 D:V1F302 4.1 52.1 1.0
N10 D:V1F302 4.1 16.3 1.0
CB D:VAL119 4.1 13.4 1.0
NE2 D:GLN89 4.1 17.4 1.0
C27 D:V1F302 4.1 44.5 1.0
O8 D:V1F302 4.2 19.2 1.0
CG1 D:VAL119 4.3 15.1 1.0
C15 D:V1F302 4.3 50.6 1.0
C31 D:V1F302 4.3 43.7 1.0
ZN D:ZN301 4.5 11.7 1.0
CG D:HIS91 4.5 12.6 1.0
CD2 D:HIS91 4.7 12.4 1.0
F12 D:V1F302 4.7 49.2 1.0
C28 D:V1F302 4.7 38.9 1.0
C20 D:V1F302 4.8 52.6 1.0
CD2 D:LEU197 4.9 13.1 1.0
CG D:GLN89 4.9 16.6 1.0
C32 D:V1F302 5.0 41.1 1.0

Reference:

V.Dudutiene, A.Zubriene, A.Smirnov, D.D.Timm, J.Smirnoviene, J.Kazokaite, V.Michailoviene, A.Zaksauskas, E.Manakova, S.Grazulis, D.Matulis. Functionalization of Fluorinated Benzenesulfonamides and Their Inhibitory Properties Toward Carbonic Anhydrases Chemmedchem V. 10 662 2015.
ISSN: ISSN 1860-7179
PubMed: 25758852
DOI: 10.1002/CMDC.201402490
Page generated: Thu Aug 1 05:16:14 2024

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