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Zinc in PDB 1dca: Structure of An Engineered Metal Binding Site in Human Carbonic Anhydrase II Reveals the Architecture of A Regulatory Cysteine Switch

Enzymatic activity of Structure of An Engineered Metal Binding Site in Human Carbonic Anhydrase II Reveals the Architecture of A Regulatory Cysteine Switch

All present enzymatic activity of Structure of An Engineered Metal Binding Site in Human Carbonic Anhydrase II Reveals the Architecture of A Regulatory Cysteine Switch:
4.2.1.1;

Protein crystallography data

The structure of Structure of An Engineered Metal Binding Site in Human Carbonic Anhydrase II Reveals the Architecture of A Regulatory Cysteine Switch, PDB code: 1dca was solved by J.A.Ippolito, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.20
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

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of An Engineered Metal Binding Site in Human Carbonic Anhydrase II Reveals the Architecture of A Regulatory Cysteine Switch (pdb code 1dca). 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 Structure of An Engineered Metal Binding Site in Human Carbonic Anhydrase II Reveals the Architecture of A Regulatory Cysteine Switch, PDB code: 1dca:

Zinc binding site 1 out of 1 in 1dca

Go back to Zinc Binding Sites List in 1dca
Zinc binding site 1 out of 1 in the Structure of An Engineered Metal Binding Site in Human Carbonic Anhydrase II Reveals the Architecture of A Regulatory Cysteine Switch


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of An Engineered Metal Binding Site in Human Carbonic Anhydrase II Reveals the Architecture of A Regulatory Cysteine Switch within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:8.3
occ:1.00
 NE2 A:HIS96 2.1 9.0 1.0
ND1 A:HIS119 2.1 5.6 1.0
NE2 A:HIS94 2.2 6.9 1.0
SG A:CYS199 2.4 8.9 1.0
CD2 A:HIS94 3.0 7.2 1.0
CD2 A:HIS96 3.0 9.4 1.0
CE1 A:HIS119 3.1 5.8 1.0
CE1 A:HIS96 3.2 9.2 1.0
CG A:HIS119 3.3 5.7 1.0
CE1 A:HIS94 3.3 7.3 1.0
CB A:CYS199 3.4 8.1 1.0
CB A:HIS119 3.7 5.4 1.0
O A:HOH314 4.2 33.0 1.0
CG A:HIS96 4.2 9.6 1.0
OE1 A:GLU106 4.2 8.7 1.0
CG A:HIS94 4.2 7.4 1.0
NE2 A:HIS119 4.3 5.5 1.0
ND1 A:HIS96 4.3 9.5 1.0
CD2 A:HIS119 4.4 5.7 1.0
ND1 A:HIS94 4.4 7.2 1.0
CD A:GLU106 4.8 8.8 1.0
CA A:CYS199 4.8 7.6 1.0

Reference:

J.A.Ippolito, D.W.Christianson. Structure of An Engineered HIS3CYS Zinc Binding Site in Human Carbonic Anhydrase II. Biochemistry V. 32 9901 1993.
ISSN: ISSN 0006-2960
PubMed: 8399159
DOI: 10.1021/BI00089A005
Page generated: Sat Oct 12 23:36:49 2024

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