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Zinc in PDB 1z97: Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer.

Enzymatic activity of Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer.

All present enzymatic activity of Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer.:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer., PDB code: 1z97 was solved by D.M.Duda, C.Tu, S.Z.Fisher, H.An, C.Yoshioka, L.Govindasamy, P.J.Laipis, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.105, 70.775, 44.487, 90.00, 115.07, 90.00
R / Rfree (%) 18.6 / 23.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer. (pdb code 1z97). 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 Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer., PDB code: 1z97:

Zinc binding site 1 out of 1 in 1z97

Go back to Zinc Binding Sites List in 1z97
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn268

b:15.0
occ:1.00
 O A:HOH278 2.0 7.1 1.0
ND1 A:HIS119 2.1 11.9 1.0
NE2 A:HIS94 2.2 12.6 1.0
NE2 A:HIS96 2.2 10.4 1.0
CE1 A:HIS119 3.0 10.2 1.0
CD2 A:HIS94 3.0 11.7 1.0
CD2 A:HIS96 3.0 10.4 1.0
CG A:HIS119 3.2 11.6 1.0
CE1 A:HIS96 3.3 11.0 1.0
CE1 A:HIS94 3.3 13.7 1.0
CB A:HIS119 3.6 10.2 1.0
O A:HOH270 3.8 10.2 1.0
OG1 A:THR199 3.8 21.1 1.0
OE1 A:GLU106 4.0 14.5 1.0
O A:HOH345 4.1 18.9 1.0
NE2 A:HIS119 4.1 13.3 1.0
CG A:HIS96 4.2 12.4 1.0
CG A:HIS94 4.2 14.1 1.0
CD2 A:HIS119 4.3 11.4 1.0
ND1 A:HIS96 4.3 13.4 1.0
ND1 A:HIS94 4.3 14.2 1.0
O A:HOH277 4.9 23.7 1.0

Reference:

D.M.Duda, C.Tu, S.Z.Fisher, H.An, C.Yoshioka, L.Govindasamy, P.J.Laipis, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer Biochemistry V. 44 10046 2005.
ISSN: ISSN 0006-2960
PubMed: 16042381
DOI: 10.1021/BI050610H
Page generated: Wed Oct 16 21:09:54 2024

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