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Zinc in PDB 1hcb: Enzyme-Substrate Interactions: Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate

Enzymatic activity of Enzyme-Substrate Interactions: Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate

All present enzymatic activity of Enzyme-Substrate Interactions: Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate:
4.2.1.1;

Protein crystallography data

The structure of Enzyme-Substrate Interactions: Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate, PDB code: 1hcb was solved by V.Kumar, K.K.Kannan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 81.850, 75.310, 37.760, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Enzyme-Substrate Interactions: Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate (pdb code 1hcb). 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 Enzyme-Substrate Interactions: Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate, PDB code: 1hcb:

Zinc binding site 1 out of 1 in 1hcb

Go back to Zinc Binding Sites List in 1hcb
Zinc binding site 1 out of 1 in the Enzyme-Substrate Interactions: Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Enzyme-Substrate Interactions: Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn261

b:8.9
occ:1.00
 O1 A:BCT522 1.8 15.9 0.4
O A:HOH521 1.8 10.3 0.3
ND1 A:HIS119 1.9 5.5 1.0
NE2 A:HIS94 2.0 6.8 1.0
NE2 A:HIS96 2.1 9.7 1.0
C A:BCT522 2.7 17.1 0.6
O A:HOH520 2.8 12.0 0.4
CE1 A:HIS119 2.9 4.5 1.0
CD2 A:HIS94 3.0 5.9 1.0
CD2 A:HIS96 3.1 5.4 1.0
CE1 A:HIS96 3.1 9.1 1.0
CE1 A:HIS94 3.1 8.0 1.0
CG A:HIS119 3.1 4.9 1.0
O3 A:BCT522 3.1 16.6 0.3
CB A:HIS119 3.6 6.5 1.0
O2 A:BCT522 3.8 17.2 0.4
OG1 A:THR199 3.9 10.7 1.0
NE2 A:HIS119 4.0 4.0 1.0
CG A:HIS94 4.2 10.6 1.0
ND1 A:HIS94 4.2 9.7 1.0
ND1 A:HIS96 4.2 6.1 1.0
CD2 A:HIS119 4.2 4.3 1.0
CG A:HIS96 4.2 7.5 1.0
OE1 A:GLU106 4.3 8.0 1.0
O A:HOH361 4.5 32.4 1.0
O A:HOH268 4.7 11.5 1.0
O A:HOH272 4.7 14.3 1.0

Reference:

V.Kumar, K.K.Kannan. Enzyme-Substrate Interactions. Structure of Human Carbonic Anhydrase I Complexed with Bicarbonate. J.Mol.Biol. V. 241 226 1994.
ISSN: ISSN 0022-2836
PubMed: 8057362
DOI: 10.1006/JMBI.1994.1491
Page generated: Wed Dec 16 02:51:03 2020

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