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Zinc in PDB 1lg5: Crystal Structure Analysis of the Hca II Mutant T199P in Complex with Beta-Mercaptoethanol

Enzymatic activity of Crystal Structure Analysis of the Hca II Mutant T199P in Complex with Beta-Mercaptoethanol

All present enzymatic activity of Crystal Structure Analysis of the Hca II Mutant T199P in Complex with Beta-Mercaptoethanol:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure Analysis of the Hca II Mutant T199P in Complex with Beta-Mercaptoethanol, PDB code: 1lg5 was solved by S.Huang, B.Sjoblom, A.E.Sauer-Eriksson, B.-H.Jonsson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 72.840, 44.803, 76.457, 90.00, 92.51, 90.00
R / Rfree (%) 20.5 / 22.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure Analysis of the Hca II Mutant T199P in Complex with Beta-Mercaptoethanol (pdb code 1lg5). 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 Crystal Structure Analysis of the Hca II Mutant T199P in Complex with Beta-Mercaptoethanol, PDB code: 1lg5:

Zinc binding site 1 out of 1 in 1lg5

Go back to Zinc Binding Sites List in 1lg5
Zinc binding site 1 out of 1 in the Crystal Structure Analysis of the Hca II Mutant T199P in Complex with Beta-Mercaptoethanol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of the Hca II Mutant T199P in Complex with Beta-Mercaptoethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:16.0
occ:1.00
 NE2 A:HIS94 2.0 13.8 1.0
NE2 A:HIS96 2.0 15.4 1.0
ND1 A:HIS119 2.1 15.0 1.0
S2 A:BME263 2.1 26.0 1.0
C2 A:BME263 2.6 30.7 1.0
CD2 A:HIS94 3.0 14.4 1.0
CD2 A:HIS96 3.0 14.6 1.0
CE1 A:HIS119 3.0 9.9 1.0
CE1 A:HIS94 3.0 12.6 1.0
CE1 A:HIS96 3.0 18.9 1.0
CG A:HIS119 3.1 12.6 1.0
CB A:HIS119 3.5 13.1 1.0
C1 A:BME263 3.5 32.5 1.0
O1 A:BME263 4.0 35.0 1.0
ND1 A:HIS94 4.1 14.7 1.0
CG A:HIS94 4.1 13.8 1.0
ND1 A:HIS96 4.1 15.3 1.0
NE2 A:HIS119 4.1 14.3 1.0
CG A:HIS96 4.1 15.0 1.0
CG A:PRO199 4.2 13.9 1.0
CD2 A:HIS119 4.2 12.2 1.0
OE1 A:GLU106 4.3 21.9 1.0
CD A:PRO199 4.8 13.5 1.0
CA A:HIS119 5.0 12.8 1.0

Reference:

S.Huang, B.Sjoblom, A.E.Sauer-Eriksson, B.H.Jonsson. Organization of An Efficient Carbonic Anhydrase: Implications For the Mechanism Based on Structure-Function Studies of A T199P/C206S Mutant. Biochemistry V. 41 7628 2002.
ISSN: ISSN 0006-2960
PubMed: 12056894
DOI: 10.1021/BI020053O
Page generated: Wed Dec 16 02:56:20 2020

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