Atomistry » Zinc » PDB 1kzy-1lg6 » 1lg6
Atomistry »
  Zinc »
    PDB 1kzy-1lg6 »
      1lg6 »

Zinc in PDB 1lg6: Crystal Structure Analysis of Hca II Mutant T199P in Complex with Thiocyanate

Enzymatic activity of Crystal Structure Analysis of Hca II Mutant T199P in Complex with Thiocyanate

All present enzymatic activity of Crystal Structure Analysis of Hca II Mutant T199P in Complex with Thiocyanate:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure Analysis of Hca II Mutant T199P in Complex with Thiocyanate, PDB code: 1lg6 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 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 66.516, 51.315, 81.003, 90.00, 107.57, 90.00
R / Rfree (%) 19.7 / 25.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure Analysis of Hca II Mutant T199P in Complex with Thiocyanate (pdb code 1lg6). 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 Hca II Mutant T199P in Complex with Thiocyanate, PDB code: 1lg6:

Zinc binding site 1 out of 1 in 1lg6

Go back to Zinc Binding Sites List in 1lg6
Zinc binding site 1 out of 1 in the Crystal Structure Analysis of Hca II Mutant T199P in Complex with Thiocyanate


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 Hca II Mutant T199P in Complex with Thiocyanate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:21.2
occ:1.00
N A:SCN263 2.0 28.0 1.0
ND1 A:HIS119 2.1 14.6 1.0
NE2 A:HIS94 2.1 17.9 1.0
NE2 A:HIS96 2.1 13.4 1.0
CE1 A:HIS94 2.8 18.2 1.0
CD2 A:HIS96 2.9 18.4 1.0
CE1 A:HIS119 3.0 11.7 1.0
C A:SCN263 3.1 27.2 1.0
CG A:HIS119 3.2 14.4 1.0
CD2 A:HIS94 3.2 17.7 1.0
CE1 A:HIS96 3.3 15.6 1.0
CB A:HIS119 3.6 14.4 1.0
O A:HOH318 3.7 24.1 1.0
CG A:PRO199 3.7 14.3 1.0
ND1 A:HIS94 4.0 17.6 1.0
NE2 A:HIS119 4.1 11.1 1.0
CG A:HIS96 4.2 16.8 1.0
OE1 A:GLU106 4.2 22.6 1.0
CG A:HIS94 4.2 16.5 1.0
CD2 A:HIS119 4.3 11.9 1.0
ND1 A:HIS96 4.3 17.9 1.0
CD A:PRO199 4.5 14.6 1.0
O A:HOH292 4.7 51.2 1.0
S A:SCN263 4.9 27.7 1.0
O A:HOH324 4.9 41.8 1.0
CB A:PRO199 5.0 17.4 1.0
CH2 A:TRP209 5.0 14.9 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: Tue Aug 19 21:32:46 2025

Last articles

Zn in 1X6F
Zn in 1X6A
Zn in 1X68
Zn in 1X64
Zn in 1X63
Zn in 1X62
Zn in 1X61
Zn in 1X5W
Zn in 1X4W
Zn in 1X4V
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy