Atomistry » Fluorine » PDB 4qte-4rv6 » 4qtl
Atomistry »
  Fluorine »
    PDB 4qte-4rv6 »
      4qtl »

Fluorine in PDB 4qtl: Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor

Enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor

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

Protein crystallography data

The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor, PDB code: 4qtl 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) 16.16 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.005, 40.913, 71.664, 90.00, 103.91, 90.00
R / Rfree (%) 16.1 / 20.3

Other elements in 4qtl:

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

Zinc (Zn) 1 atom

Fluorine Binding Sites:

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

Fluorine binding site 1 out of 3 in 4qtl

Go back to Fluorine Binding Sites List in 4qtl
Fluorine binding site 1 out of 3 in the Crystal Structure of Human Carbonic Anhydrase Isozyme II 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 Human Carbonic Anhydrase Isozyme II with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F304

b:21.6
occ:1.00
F27 A:WWO304 0.0 21.6 1.0
C5 A:WWO304 1.4 31.9 1.0
C6 A:WWO304 2.4 34.6 1.0
C4 A:WWO304 2.4 30.1 1.0
N10 A:WWO304 2.7 21.0 1.0
O A:HOH554 2.8 24.2 1.0
N26 A:WWO304 2.9 36.6 1.0
S7 A:WWO304 3.2 28.2 1.0
OG1 A:THR200 3.2 14.5 1.0
NE2 A:HIS94 3.3 7.2 1.0
CE1 A:HIS94 3.5 8.0 1.0
ZN A:ZN301 3.6 7.4 1.0
CG2 A:THR200 3.6 12.9 1.0
C3 A:WWO304 3.7 34.9 1.0
C1 A:WWO304 3.7 38.9 1.0
O A:HOH555 3.9 29.2 1.0
CB A:THR200 4.0 11.9 1.0
CD2 A:HIS94 4.1 7.5 1.0
C2 A:WWO304 4.1 33.8 1.0
O9 A:WWO304 4.2 25.1 1.0
C14 A:WWO304 4.3 34.4 1.0
O8 A:WWO304 4.3 22.1 1.0
ND1 A:HIS94 4.3 7.8 1.0
NE2 A:HIS96 4.5 7.8 1.0
CE1 A:HIS96 4.5 7.8 1.0
O A:HOH605 4.6 34.0 1.0
OG1 A:THR199 4.6 6.8 1.0
N A:THR200 4.7 9.4 1.0
CG A:HIS94 4.7 7.4 1.0
F12 A:WWO304 4.8 35.0 1.0
C20 A:WWO304 4.9 34.3 0.0
O A:HOH553 5.0 25.0 1.0
CA A:THR200 5.0 10.0 1.0

Fluorine binding site 2 out of 3 in 4qtl

Go back to Fluorine Binding Sites List in 4qtl
Fluorine binding site 2 out of 3 in the Crystal Structure of Human Carbonic Anhydrase Isozyme II 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 Human Carbonic Anhydrase Isozyme II with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F304

b:35.0
occ:1.00
F12 A:WWO304 0.0 35.0 1.0
C3 A:WWO304 1.4 34.9 1.0
C2 A:WWO304 2.4 33.8 1.0
C4 A:WWO304 2.4 30.1 1.0
F13 A:WWO304 2.6 39.5 1.0
S7 A:WWO304 2.9 28.2 1.0
O9 A:WWO304 2.9 25.1 1.0
O8 A:WWO304 3.1 22.1 1.0
CD2 A:LEU198 3.2 14.1 1.0
C1 A:WWO304 3.6 38.9 1.0
CG2 A:VAL121 3.7 7.3 1.0
C5 A:WWO304 3.7 31.9 1.0
CG2 A:VAL143 3.7 7.1 1.0
CG1 A:VAL121 3.7 7.7 1.0
CD1 A:LEU141 4.0 10.5 1.0
C6 A:WWO304 4.2 34.6 1.0
CB A:VAL121 4.3 7.3 1.0
CG A:LEU198 4.5 11.6 1.0
N10 A:WWO304 4.6 21.0 1.0
CA A:LEU198 4.7 8.3 1.0
CB A:LEU198 4.7 9.8 1.0
F27 A:WWO304 4.8 21.6 1.0
CG1 A:VAL143 4.8 6.8 1.0
CE1 A:HIS94 4.8 8.0 1.0
CB A:VAL143 4.9 7.1 1.0
CG2 A:VAL207 4.9 7.1 1.0

Fluorine binding site 3 out of 3 in 4qtl

Go back to Fluorine Binding Sites List in 4qtl
Fluorine binding site 3 out of 3 in the Crystal Structure of Human Carbonic Anhydrase Isozyme II 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 Human Carbonic Anhydrase Isozyme II with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F304

b:39.5
occ:1.00
F13 A:WWO304 0.0 39.5 1.0
C2 A:WWO304 1.4 33.8 1.0
C3 A:WWO304 2.3 34.9 1.0
C1 A:WWO304 2.4 38.9 1.0
F12 A:WWO304 2.6 35.0 1.0
O23 A:WWO304 2.8 52.4 1.0
S11 A:WWO304 2.9 46.9 1.0
CG1 A:VAL121 3.1 7.7 1.0
CZ A:PHE131 3.2 17.7 1.0
CE1 A:PHE131 3.4 16.2 1.0
C4 A:WWO304 3.6 30.1 1.0
C21 A:WWO304 3.7 43.2 1.0
C6 A:WWO304 3.7 34.6 1.0
CD1 A:LEU141 3.7 10.5 1.0
CD2 A:LEU198 3.7 14.1 1.0
NE2 A:GLN92 4.0 11.7 0.5
CG2 A:VAL121 4.0 7.3 1.0
CB A:VAL121 4.0 7.3 1.0
C5 A:WWO304 4.1 31.9 1.0
O22 A:WWO304 4.3 49.4 1.0
CE2 A:PHE131 4.4 18.0 1.0
CD1 A:PHE131 4.7 13.2 1.0
N26 A:WWO304 4.9 36.6 1.0
C24 A:WWO304 5.0 52.6 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: Sun Dec 13 12:11:49 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy