Atomistry » Zinc » PDB 1zs0-2a21 » 1zsb
Atomistry »
  Zinc »
    PDB 1zs0-2a21 »
      1zsb »

Zinc in PDB 1zsb: Carbonic Anhydrase II Mutant E117Q, Transition State Analogue Acetazolamide

Enzymatic activity of Carbonic Anhydrase II Mutant E117Q, Transition State Analogue Acetazolamide

All present enzymatic activity of Carbonic Anhydrase II Mutant E117Q, Transition State Analogue Acetazolamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II Mutant E117Q, Transition State Analogue Acetazolamide, PDB code: 1zsb was solved by C.A.Lesburg, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) 16.4 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Carbonic Anhydrase II Mutant E117Q, Transition State Analogue Acetazolamide (pdb code 1zsb). 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 Carbonic Anhydrase II Mutant E117Q, Transition State Analogue Acetazolamide, PDB code: 1zsb:

Zinc binding site 1 out of 1 in 1zsb

Go back to Zinc Binding Sites List in 1zsb
Zinc binding site 1 out of 1 in the Carbonic Anhydrase II Mutant E117Q, Transition State Analogue Acetazolamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carbonic Anhydrase II Mutant E117Q, Transition State Analogue Acetazolamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:19.7
occ:1.00
ND1 A:HIS119 1.9 5.5 1.0
NE2 A:HIS94 2.0 9.6 1.0
NE2 A:HIS96 2.1 5.3 1.0
N1 A:AZM264 2.1 17.1 1.0
CE1 A:HIS119 2.8 5.0 1.0
CD2 A:HIS94 2.9 8.2 1.0
CD2 A:HIS96 3.0 5.0 1.0
CG A:HIS119 3.1 6.0 1.0
S1 A:AZM264 3.1 18.1 1.0
O2 A:AZM264 3.1 16.5 1.0
CE1 A:HIS94 3.1 9.8 1.0
CE1 A:HIS96 3.2 5.0 1.0
CB A:HIS119 3.5 5.8 1.0
OG1 A:THR199 3.8 7.6 1.0
OE1 A:GLU106 3.9 7.3 1.0
NE2 A:HIS119 4.0 6.9 1.0
CG A:HIS94 4.1 9.3 1.0
CD2 A:HIS119 4.1 5.7 1.0
O1 A:AZM264 4.2 17.1 1.0
C1 A:AZM264 4.2 19.3 1.0
ND1 A:HIS94 4.2 8.3 1.0
CG A:HIS96 4.2 6.2 1.0
ND1 A:HIS96 4.3 5.3 1.0
CD A:GLU106 4.9 8.1 1.0
N3 A:AZM264 4.9 20.9 1.0
CA A:HIS119 5.0 6.7 1.0

Reference:

C.C.Huang, C.A.Lesburg, L.L.Kiefer, C.A.Fierke, D.W.Christianson. Reversal of the Hydrogen Bond to Zinc Ligand Histidine-119 Dramatically Diminishes Catalysis and Enhances Metal Equilibration Kinetics in Carbonic Anhydrase II. Biochemistry V. 35 3439 1996.
ISSN: ISSN 0006-2960
PubMed: 8639494
DOI: 10.1021/BI9526692
Page generated: Wed Dec 16 03:16:11 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy