Atomistry » Zinc » PDB 3gtv-3h68 » 3gz0
Atomistry »
  Zinc »
    PDB 3gtv-3h68 »
      3gz0 »

Zinc in PDB 3gz0: Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability and Solvent Network

Enzymatic activity of Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability and Solvent Network

All present enzymatic activity of Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability and Solvent Network:
4.2.1.1;

Protein crystallography data

The structure of Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability and Solvent Network, PDB code: 3gz0 was solved by B.S.Avvaru, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.26
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.737, 41.623, 72.821, 90.00, 104.59, 90.00
R / Rfree (%) 14 / 18.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability and Solvent Network (pdb code 3gz0). 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 Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability and Solvent Network, PDB code: 3gz0:

Zinc binding site 1 out of 1 in 3gz0

Go back to Zinc Binding Sites List in 3gz0
Zinc binding site 1 out of 1 in the Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability and Solvent Network


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability and Solvent Network within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:12.5
occ:0.10
 O A:HOH2001 1.5 23.3 1.0
NE2 A:HIS94 2.0 21.0 1.0
NE2 A:HIS96 2.2 15.3 1.0
ND1 A:HIS119 2.2 11.9 1.0
CE1 A:HIS94 2.9 21.1 1.0
CE1 A:HIS119 3.0 11.1 1.0
CD2 A:HIS94 3.0 19.2 1.0
CD2 A:HIS96 3.1 13.6 1.0
CE1 A:HIS96 3.3 15.3 1.0
CG A:HIS119 3.3 10.2 1.0
O A:HOH2075 3.3 32.6 1.0
OG1 A:THR199 3.7 10.9 1.0
CB A:HIS119 3.7 9.9 1.0
ND1 A:HIS94 4.0 18.4 1.0
O A:HOH2104 4.0 36.5 1.0
OE1 A:GLU106 4.1 11.9 1.0
CG A:HIS94 4.1 16.2 1.0
NE2 A:HIS119 4.2 10.7 1.0
CG A:HIS96 4.3 11.7 1.0
ND1 A:HIS96 4.3 12.7 1.0
CD2 A:HIS119 4.3 10.6 1.0
O A:HOH2095 4.6 33.1 1.0
O A:HOH2169 4.6 42.0 1.0
CD A:GLU106 5.0 11.1 1.0

Reference:

B.S.Avvaru, S.A.Busby, M.J.Chalmers, P.R.Griffin, B.Venkatakrishnan, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of A Metal in Protein Structure, Stability, and Solvent Network . Biochemistry V. 48 7365 2009.
ISSN: ISSN 0006-2960
PubMed: 19583303
DOI: 10.1021/BI9007512
Page generated: Thu Oct 24 14:03:12 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