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Zinc in PDB 1lzv: Site-Specific Mutant (TYR7 Replaced with His) of Human Carbonic Anhydrase II

Enzymatic activity of Site-Specific Mutant (TYR7 Replaced with His) of Human Carbonic Anhydrase II

All present enzymatic activity of Site-Specific Mutant (TYR7 Replaced with His) of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Site-Specific Mutant (TYR7 Replaced with His) of Human Carbonic Anhydrase II, PDB code: 1lzv was solved by C.K.Tu, M.Qian, H.An, N.R.Wadhwa, D.M.Duda, C.Yoshioka, Y.Pathak, R.Mckenna, P.J.Laipis, D.N.Silverman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.871, 41.585, 72.951, 90.00, 104.75, 90.00
R / Rfree (%) 18.6 / 25.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Site-Specific Mutant (TYR7 Replaced with His) of Human Carbonic Anhydrase II (pdb code 1lzv). 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 Site-Specific Mutant (TYR7 Replaced with His) of Human Carbonic Anhydrase II, PDB code: 1lzv:

Zinc binding site 1 out of 1 in 1lzv

Go back to Zinc Binding Sites List in 1lzv
Zinc binding site 1 out of 1 in the Site-Specific Mutant (TYR7 Replaced with His) 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 Site-Specific Mutant (TYR7 Replaced with His) of Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:17.5
occ:1.00
ND1 A:HIS119 2.0 13.4 1.0
NE2 A:HIS94 2.1 14.7 1.0
NE2 A:HIS96 2.1 13.3 1.0
O A:HOH301 2.7 15.6 1.0
CE1 A:HIS119 2.8 12.2 1.0
CD2 A:HIS96 3.0 14.1 1.0
CE1 A:HIS94 3.0 13.5 1.0
CD2 A:HIS94 3.1 13.9 1.0
CG A:HIS119 3.1 13.9 1.0
CE1 A:HIS96 3.2 13.9 1.0
CB A:HIS119 3.6 12.1 1.0
OG1 A:THR199 3.6 18.0 1.0
NE2 A:HIS119 4.0 10.5 1.0
OE1 A:GLU106 4.0 14.9 1.0
ND1 A:HIS94 4.1 12.3 1.0
CD2 A:HIS119 4.2 12.6 1.0
CG A:HIS96 4.2 15.6 1.0
CG A:HIS94 4.2 12.3 1.0
ND1 A:HIS96 4.2 14.4 1.0
CD A:GLU106 4.8 15.0 1.0

Reference:

C.Tu, M.Qian, H.An, N.R.Wadhwa, D.Duda, C.Yoshioka, Y.Pathak, R.Mckenna, P.J.Laipis, D.N.Silverman. Kinetic Analysis of Multiple Proton Shuttles in the Active Site of Human Carbonic Anhydrase. J.Biol.Chem. V. 277 38870 2002.
ISSN: ISSN 0021-9258
PubMed: 12171926
DOI: 10.1074/JBC.M205791200
Page generated: Wed Dec 16 02:56:32 2020

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