Atomistry » Zinc » PDB 3dsv-3e2c » 3dv7
Atomistry »
  Zinc »
    PDB 3dsv-3e2c »
      3dv7 »

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: Thu Oct 24 12:20:37 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy