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Atomistry » Zinc » PDB 1gkr-1h4t » 1gxw | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1gkr-1h4t » 1gxw » |
Zinc in PDB 1gxw: The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium ThiocyanateEnzymatic activity of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate
All present enzymatic activity of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate:
3.4.24.27; Protein crystallography data
The structure of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate, PDB code: 1gxw
was solved by
J.F.Gaucher,
M.Selkti,
T.Prange,
A.Tomas,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1gxw:
The structure of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate
(pdb code 1gxw). 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 The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate, PDB code: 1gxw: Zinc binding site 1 out of 1 in 1gxwGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate
![]() Mono view ![]() Stereo pair view
Reference:
J.Gaucher,
M.Selkti,
T.Prange,
A.Tomas.
The 2.2 A Resolution Structure of Thermolysin (Tln) Crystallized in the Presence of Potassium Thiocyanate. Acta Crystallogr.,Sect.D V. 58 2198 2002.
Page generated: Sun Oct 13 01:48:41 2024
ISSN: ISSN 0907-4449 PubMed: 12454500 DOI: 10.1107/S0907444902015457 |
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