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Zinc in PDB 1h9n: H119N Carbonic Anhydrase II

Enzymatic activity of H119N Carbonic Anhydrase II

All present enzymatic activity of H119N Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of H119N Carbonic Anhydrase II, PDB code: 1h9n was solved by C.A.Lesburg, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.85
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 (%) 17 / 23.6

Zinc Binding Sites:

The binding sites of Zinc atom in the H119N Carbonic Anhydrase II (pdb code 1h9n). 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 H119N Carbonic Anhydrase II, PDB code: 1h9n:

Zinc binding site 1 out of 1 in 1h9n

Go back to Zinc Binding Sites List in 1h9n
Zinc binding site 1 out of 1 in the H119N 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 H119N Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:18.4
occ:1.00
NE2 A:HIS96 2.0 12.4 1.0
NE2 A:HIS94 2.0 15.3 1.0
O A:HOH300 2.1 20.6 1.0
O A:HOH301 2.2 15.7 1.0
OD1 A:ASN119 2.3 17.2 1.0
CD2 A:HIS94 3.0 13.8 1.0
CD2 A:HIS96 3.0 11.2 1.0
CE1 A:HIS96 3.0 10.8 1.0
CE1 A:HIS94 3.1 14.2 1.0
CG A:ASN119 3.4 16.1 1.0
OG1 A:THR199 3.8 13.0 1.0
CB A:ASN119 3.9 14.2 1.0
OE1 A:GLU106 4.0 14.2 1.0
O A:HOH456 4.1 27.8 1.0
O A:HOH367 4.1 17.3 1.0
ND1 A:HIS96 4.2 11.3 1.0
CG A:HIS96 4.2 12.3 1.0
CG A:HIS94 4.2 13.8 1.0
ND1 A:HIS94 4.2 14.4 1.0
O A:HOH373 4.4 30.1 1.0
ND2 A:ASN119 4.5 15.8 1.0
CD A:GLU106 4.8 13.9 1.0

Reference:

C.A.Lesburg, C.Huang, D.W.Christianson, C.A.Fierke. Histidine --> Carboxamide Ligand Substitutions in the Zinc Binding Site of Carbonic Anhydrase II Alter Metal Coordination Geometry But Retain Catalytic Activity. Biochemistry V. 36 15780 1997.
ISSN: ISSN 0006-2960
PubMed: 9398308
DOI: 10.1021/BI971296X
Page generated: Sun Oct 13 02:04:34 2024

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