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Zinc in PDB 3dv7: Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II (N62A)

Enzymatic activity of Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II (N62A)

All present enzymatic activity of Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II (N62A):
4.2.1.1;

Protein crystallography data

The structure of Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II (N62A), PDB code: 3dv7 was solved by B.S.Avvaru, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.04 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.812, 41.774, 72.951, 90.00, 104.62, 90.00
R / Rfree (%) 17.9 / 19.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II (N62A) (pdb code 3dv7). 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 Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II (N62A), PDB code: 3dv7:

Zinc binding site 1 out of 1 in 3dv7

Go back to Zinc Binding Sites List in 3dv7
Zinc binding site 1 out of 1 in the Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II (N62A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II (N62A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:11.9
occ:1.00
 NE2 A:HIS94 2.1 9.5 1.0
NE2 A:HIS96 2.1 10.1 1.0
ND1 A:HIS119 2.1 8.7 1.0
O A:HOH277 2.2 17.3 1.0
CE1 A:HIS119 3.0 10.8 1.0
CD2 A:HIS94 3.0 10.6 1.0
CD2 A:HIS96 3.0 10.4 1.0
CE1 A:HIS94 3.1 12.2 1.0
CE1 A:HIS96 3.2 10.2 1.0
CG A:HIS119 3.2 8.0 1.0
CB A:HIS119 3.6 8.0 1.0
O A:HOH274 3.7 21.1 1.0
OG1 A:THR199 3.8 12.1 1.0
OE1 A:GLU106 4.0 12.0 1.0
O A:HOH300 4.0 24.5 1.0
NE2 A:HIS119 4.1 9.0 1.0
CG A:HIS94 4.2 10.2 1.0
ND1 A:HIS94 4.2 10.6 1.0
O A:HOH303 4.2 26.0 1.0
CG A:HIS96 4.2 8.4 1.0
ND1 A:HIS96 4.2 10.2 1.0
CD2 A:HIS119 4.3 9.3 1.0
CD A:GLU106 4.9 11.3 1.0

Reference:

J.Zheng, B.S.Avvaru, C.Tu, R.Mckenna, D.N.Silverman. Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II. Biochemistry V. 47 12028 2008.
ISSN: ISSN 0006-2960
PubMed: 18942852
DOI: 10.1021/BI801473W
Page generated: Wed Dec 16 04:13:59 2020

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