Atomistry » Zinc » PDB 1y8f-1yj6 » 1ydd
Atomistry »
  Zinc »
    PDB 1y8f-1yj6 »
      1ydd »

Zinc in PDB 1ydd: Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II

Enzymatic activity of Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II

All present enzymatic activity of Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II, PDB code: 1ydd was solved by S.K.Nair, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.50 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1ydd:

The structure of Structural Basis of Inhibitor Affinity to Variants of 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 Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II (pdb code 1ydd). 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 Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II, PDB code: 1ydd:

Zinc binding site 1 out of 1 in 1ydd

Go back to Zinc Binding Sites List in 1ydd
Zinc binding site 1 out of 1 in the Structural Basis of Inhibitor Affinity to Variants of 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 Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:4.3
occ:1.00
 N1 A:AZM264 1.7 9.9 1.0
NE2 A:HIS96 1.9 0.5 1.0
ND1 A:HIS119 2.1 3.1 1.0
NE2 A:HIS94 2.3 3.2 1.0
CE1 A:HIS119 2.8 3.5 1.0
CD2 A:HIS96 2.9 0.5 1.0
CE1 A:HIS96 2.9 0.5 1.0
CD2 A:HIS94 3.1 3.1 1.0
S1 A:AZM264 3.1 9.9 1.0
CG A:HIS119 3.1 3.0 1.0
CE1 A:HIS94 3.4 3.4 1.0
O2 A:AZM264 3.5 9.7 1.0
CB A:HIS119 3.6 2.8 1.0
OG1 A:THR199 3.8 6.7 1.0
OE1 A:GLU106 3.9 5.6 1.0
ND1 A:HIS96 4.0 0.5 1.0
O1 A:AZM264 4.0 10.2 1.0
CG A:HIS96 4.0 0.5 1.0
C1 A:AZM264 4.0 10.3 1.0
NE2 A:HIS119 4.1 3.4 1.0
N3 A:AZM264 4.2 10.6 1.0
CD2 A:HIS119 4.2 3.0 1.0
CG A:HIS94 4.3 3.5 1.0
ND1 A:HIS94 4.5 3.1 1.0
O A:HOH342 4.6 27.8 1.0
CD A:GLU106 4.7 5.9 1.0

Reference:

S.K.Nair, J.F.Krebs, D.W.Christianson, C.A.Fierke. Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II. Biochemistry V. 34 3981 1995.
ISSN: ISSN 0006-2960
PubMed: 7696263
DOI: 10.1021/BI00012A016
Page generated: Wed Oct 16 20:52:43 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy