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Zinc in PDB 2hfw: Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III

Enzymatic activity of Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III

All present enzymatic activity of Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III:
4.2.1.1;

Protein crystallography data

The structure of Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III, PDB code: 2hfw was solved by I.Elder, S.Z.Fisher, P.J.Laipis, C.K.Tu, R.Mckenna, D.N.Silverman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.373, 51.674, 117.659, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 23.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III (pdb code 2hfw). 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 Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III, PDB code: 2hfw:

Zinc binding site 1 out of 1 in 2hfw

Go back to Zinc Binding Sites List in 2hfw
Zinc binding site 1 out of 1 in the Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:26.9
occ:1.00
 ND1 A:HIS119 2.1 16.4 1.0
NE2 A:HIS96 2.1 22.3 1.0
CE1 A:HIS94 2.6 24.3 1.0
O A:HOH326 2.7 18.9 1.0
CE1 A:HIS119 2.8 14.3 1.0
CE1 A:HIS96 3.0 23.6 1.0
CD2 A:HIS96 3.1 23.4 1.0
CG A:HIS119 3.2 15.7 1.0
ND1 A:HIS94 3.4 24.9 1.0
NE2 A:HIS94 3.6 24.4 1.0
CB A:HIS119 3.6 15.5 1.0
O A:HOH387 3.9 38.8 1.0
NE2 A:HIS119 4.0 16.8 1.0
OG1 A:THR199 4.0 25.3 1.0
ND1 A:HIS96 4.1 23.8 1.0
OE1 A:GLU106 4.2 25.4 1.0
CD2 A:HIS119 4.2 15.2 1.0
CG A:HIS96 4.2 24.4 1.0
CG A:HIS94 4.5 27.5 1.0
CD2 A:HIS94 4.6 26.2 1.0

Reference:

I.Elder, Z.Fisher, P.J.Laipis, C.Tu, R.Mckenna, D.N.Silverman. Structural and Kinetic Analysis of Proton Shuttle Residues in the Active Site of Human Carbonic Anhydrase III. Proteins V. 68 337 2007.
ISSN: ISSN 0887-3585
PubMed: 17427958
DOI: 10.1002/PROT.21403
Page generated: Wed Dec 16 03:30:09 2020

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