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Zinc in PDB 1yda: 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: 1yda 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 1yda:

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 1yda). 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: 1yda:

Zinc binding site 1 out of 1 in 1yda

Go back to Zinc Binding Sites List in 1yda
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:8.0
occ:1.00
 NE2 A:HIS96 2.2 2.0 1.0
ND1 A:HIS119 2.3 2.0 1.0
O2 A:AZM264 2.5 3.8 1.0
NE2 A:HIS94 2.6 2.3 1.0
N1 A:AZM264 2.8 3.1 1.0
CD2 A:HIS94 2.8 2.0 1.0
CE1 A:HIS96 2.9 2.0 1.0
S1 A:AZM264 3.0 3.4 1.0
CE1 A:HIS119 3.1 2.0 1.0
CG A:HIS119 3.3 2.0 1.0
CD2 A:HIS96 3.3 2.0 1.0
O A:HOH340 3.5 20.2 1.0
CB A:HIS119 3.8 2.0 1.0
CE1 A:HIS94 3.9 3.9 1.0
OE1 A:GLU106 4.0 2.0 1.0
OG1 A:THR199 4.0 8.3 1.0
O1 A:AZM264 4.1 5.2 1.0
ND1 A:HIS96 4.1 2.0 1.0
NE2 A:HIS119 4.2 2.5 1.0
CG A:HIS94 4.2 4.8 1.0
C1 A:AZM264 4.3 2.0 1.0
CG A:HIS96 4.3 2.0 1.0
CD2 A:HIS119 4.3 3.5 1.0
ND1 A:HIS94 4.7 2.1 1.0
CD A:GLU106 4.9 2.1 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 Dec 16 03:14:04 2020

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