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Zinc in PDB 1g0f: Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II

Enzymatic activity of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II

All present enzymatic activity of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II, PDB code: 1g0f was solved by D.Duda, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.484, 41.616, 72.658, 90.00, 104.52, 90.00
R / Rfree (%) 17.9 / 19.8

Other elements in 1g0f:

The structure of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II (pdb code 1g0f). 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 (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II, PDB code: 1g0f:

Zinc binding site 1 out of 1 in 1g0f

Go back to Zinc Binding Sites List in 1g0f
Zinc binding site 1 out of 1 in the Site-Specific Mutant (HIS64 Replaced with Ala) 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 (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:10.2
occ:1.00
 ND1 A:HIS119 2.1 8.6 1.0
NE2 A:HIS96 2.1 9.9 1.0
NE2 A:HIS94 2.1 9.8 1.0
O A:HOH428 2.3 43.1 1.0
CE1 A:HIS119 2.9 7.8 1.0
CD2 A:HIS96 3.0 10.8 1.0
CD2 A:HIS94 3.0 9.5 1.0
CE1 A:HIS94 3.1 10.4 1.0
CE1 A:HIS96 3.1 9.9 1.0
CG A:HIS119 3.2 7.6 1.0
OG1 A:THR199 3.5 12.7 1.0
CB A:HIS119 3.6 8.6 1.0
O A:HOH326 3.7 26.9 1.0
OE1 A:GLU106 4.0 13.1 1.0
NE2 A:HIS119 4.1 7.8 1.0
CG A:HIS96 4.2 8.5 1.0
CG A:HIS94 4.2 9.3 1.0
ND1 A:HIS94 4.2 10.1 1.0
ND1 A:HIS96 4.2 9.6 1.0
CD2 A:HIS119 4.2 10.2 1.0
O A:HOH323 4.4 28.8 1.0
CD A:GLU106 4.9 13.0 1.0
CB A:THR199 4.9 12.3 1.0

Reference:

D.Duda, C.Tu, M.Qian, P.Laipis, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. Structural and Kinetic Analysis of the Chemical Rescue of the Proton Transfer Function of Carbonic Anhydrase II. Biochemistry V. 40 1741 2001.
ISSN: ISSN 0006-2960
PubMed: 11327835
DOI: 10.1021/BI002295Z
Page generated: Sun Oct 13 01:13:59 2024

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