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Zinc in PDB 4jsw: Human Carbonic Anhydrase II H94C

Enzymatic activity of Human Carbonic Anhydrase II H94C

All present enzymatic activity of Human Carbonic Anhydrase II H94C:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II H94C, PDB code: 4jsw was solved by D.P.Martin, Z.S.Hann, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.42 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.596, 41.086, 71.957, 90.00, 103.66, 90.00
R / Rfree (%) 21.9 / 28.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II H94C (pdb code 4jsw). 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 Human Carbonic Anhydrase II H94C, PDB code: 4jsw:

Zinc binding site 1 out of 1 in 4jsw

Go back to Zinc Binding Sites List in 4jsw
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II H94C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II H94C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:4.3
occ:1.00
NE2 A:HIS96 2.0 4.7 1.0
O A:HOH401 2.0 2.0 1.0
ND1 A:HIS119 2.1 2.0 1.0
SG A:CYS94 2.2 3.7 1.0
CE1 A:HIS96 3.0 2.0 1.0
CD2 A:HIS96 3.0 5.4 1.0
CE1 A:HIS119 3.0 2.0 1.0
CG A:HIS119 3.1 2.0 1.0
CB A:CYS94 3.3 7.6 1.0
CB A:HIS119 3.5 2.0 1.0
C A:CYS94 4.1 6.2 1.0
ND1 A:HIS96 4.1 3.6 1.0
O A:CYS94 4.1 5.5 1.0
CG A:HIS96 4.1 2.9 1.0
NE2 A:HIS119 4.1 2.0 1.0
CD2 A:HIS119 4.2 2.0 1.0
OE1 A:GLU106 4.2 2.0 1.0
CA A:CYS94 4.2 5.4 1.0
OG1 A:THR199 4.4 2.0 1.0
N A:PHE95 4.6 4.6 1.0
CA A:HIS119 4.8 2.0 1.0
N A:HIS119 4.8 2.0 1.0
N A:CYS94 4.8 5.6 1.0

Reference:

D.P.Martin, Z.S.Hann, S.M.Cohen. Metalloprotein-Inhibitor Binding: Human Carbonic Anhydrase II As A Model For Probing Metal-Ligand Interactions in A Metalloprotein Active Site. Inorg.Chem. V. 52 12207 2013.
ISSN: ISSN 0020-1669
PubMed: 23706138
DOI: 10.1021/IC400295F
Page generated: Sun Oct 27 01:29:37 2024

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