Atomistry » Zinc » PDB 4q30-4q8u » 4q7s
Atomistry »
  Zinc »
    PDB 4q30-4q8u »
      4q7s »

Zinc in PDB 4q7s: Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II

Enzymatic activity of Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II

All present enzymatic activity of Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II, PDB code: 4q7s was solved by D.P.Martin, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.84 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.113, 41.418, 71.987, 90.00, 104.12, 90.00
R / Rfree (%) 18.9 / 22.6

Other elements in 4q7s:

The structure of Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II (pdb code 4q7s). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II, PDB code: 4q7s:

Zinc binding site 1 out of 1 in 4q7s

Go back to Zinc Binding Sites List in 4q7s
Zinc binding site 1 out of 1 in the Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of 1-Hydroxy-4-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:9.6
occ:1.00
 NE2 A:HIS96 2.1 7.3 1.0
NE2 A:HIS94 2.1 8.8 1.0
ND1 A:HIS119 2.2 7.5 1.0
S1 A:2YU302 2.4 11.4 1.0
O1 A:2YU302 2.4 13.7 1.0
N1 A:2YU302 3.0 11.9 1.0
C1 A:2YU302 3.0 11.2 1.0
CD2 A:HIS94 3.0 13.0 1.0
CE1 A:HIS96 3.0 11.2 1.0
CE1 A:HIS119 3.1 6.0 1.0
CD2 A:HIS96 3.1 9.6 1.0
CE1 A:HIS94 3.1 7.3 1.0
CG A:HIS119 3.3 6.3 1.0
OG1 A:THR199 3.5 6.6 1.0
CB A:HIS119 3.7 5.1 1.0
OE1 A:GLU106 4.0 7.6 1.0
ND1 A:HIS96 4.2 6.9 1.0
O A:HOH404 4.2 9.4 1.0
CG A:HIS94 4.2 8.1 1.0
ND1 A:HIS94 4.2 7.3 1.0
CG A:HIS96 4.2 5.6 1.0
NE2 A:HIS119 4.3 4.2 1.0
C5 A:2YU302 4.3 11.8 1.0
C2 A:2YU302 4.3 10.9 1.0
CD2 A:HIS119 4.4 8.1 1.0
CB A:THR199 4.9 6.4 1.0

Reference:

D.P.Martin, P.G.Blachly, J.A.Mccammon, S.M.Cohen. Exploring the Influence of the Protein Environment on Metal-Binding Pharmacophores. J.Med.Chem. V. 57 7126 2014.
ISSN: ISSN 0022-2623
PubMed: 25116076
DOI: 10.1021/JM500984B
Page generated: Wed Dec 16 05:42:46 2020

Last articles

Zn in 8PFC
Zn in 8SF0
Zn in 8SOJ
Zn in 8SOK
Zn in 8SYI
Zn in 8SLG
Zn in 8SEX
Zn in 8SEZ
Zn in 8SJG
Zn in 8SEY
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy