Atomistry » Zinc » PDB 1z5r-1zfo » 1z93
Atomistry »
  Zinc »
    PDB 1z5r-1zfo »
      1z93 »

Zinc in PDB 1z93: 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: 1z93 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 65
Cell size a, b, c (Å), α, β, γ (°) 44.700, 44.700, 222.557, 90.00, 90.00, 120.00
R / Rfree (%) 20.5 / 25.8

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 1z93). 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: 1z93:

Zinc binding site 1 out of 1 in 1z93

Go back to Zinc Binding Sites List in 1z93
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:18.7
occ:1.00
NE2 A:HIS94 2.0 18.5 1.0
O A:HOH269 2.0 14.6 1.0
ND1 A:HIS119 2.1 7.4 1.0
NE2 A:HIS96 2.3 21.6 1.0
CE1 A:HIS119 2.9 8.9 1.0
CD2 A:HIS94 2.9 15.8 1.0
CD2 A:HIS96 2.9 19.6 1.0
CE1 A:HIS94 3.0 19.7 1.0
CG A:HIS119 3.1 11.7 1.0
CE1 A:HIS96 3.4 21.7 1.0
CB A:HIS119 3.6 11.5 1.0
OG1 A:THR199 3.6 18.4 1.0
O A:HOH292 4.0 26.2 1.0
NE2 A:HIS119 4.1 11.0 1.0
CG A:HIS94 4.1 19.9 1.0
ND1 A:HIS94 4.1 19.2 1.0
CG A:HIS96 4.2 20.5 1.0
CD2 A:HIS119 4.2 10.3 1.0
OE1 A:GLU106 4.2 18.1 1.0
ND1 A:HIS96 4.4 18.9 1.0
O A:HOH326 4.7 19.8 1.0
CB A:THR199 4.9 18.8 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 21:09:39 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy