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Atomistry » Zinc » PDB 1lg5-1m2j » 1lnd | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1lg5-1m2j » 1lnd » |
Zinc in PDB 1lnd: A Structural Analysis of Metal Substitutions in ThermolysinEnzymatic activity of A Structural Analysis of Metal Substitutions in Thermolysin
All present enzymatic activity of A Structural Analysis of Metal Substitutions in Thermolysin:
3.4.24.27; Protein crystallography data
The structure of A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lnd
was solved by
D.R.Holland,
A.C.Hausrath,
D.Juers,
B.W.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1lnd:
The structure of A Structural Analysis of Metal Substitutions in Thermolysin also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the A Structural Analysis of Metal Substitutions in Thermolysin
(pdb code 1lnd). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lnd: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1lndGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the A Structural Analysis of Metal Substitutions in Thermolysin
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 1lndGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the A Structural Analysis of Metal Substitutions in Thermolysin
![]() Mono view ![]() Stereo pair view
Reference:
D.R.Holland,
A.C.Hausrath,
D.Juers,
B.W.Matthews.
Structural Analysis of Zinc Substitutions in the Active Site of Thermolysin. Protein Sci. V. 4 1955 1995.
Page generated: Wed Dec 16 02:56:23 2020
ISSN: ISSN 0961-8368 PubMed: 8535232 |
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