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Atomistry » Zinc » PDB 1my2-1ndy » 1n19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1my2-1ndy » 1n19 » |
Zinc in PDB 1n19: Structure of the Hsod A4V MutantEnzymatic activity of Structure of the Hsod A4V Mutant
All present enzymatic activity of Structure of the Hsod A4V Mutant:
1.15.1.1; Protein crystallography data
The structure of Structure of the Hsod A4V Mutant, PDB code: 1n19
was solved by
R.M.F.Cardoso,
M.M.Thayer,
M.Didonato,
T.P.Lo,
C.K.Bruns,
E.D.Getzoff,
J.A.Tainer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1n19:
The structure of Structure of the Hsod A4V Mutant also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of the Hsod A4V Mutant
(pdb code 1n19). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the Hsod A4V Mutant, PDB code: 1n19: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1n19Go back to![]() ![]()
Zinc binding site 1 out
of 2 in the Structure of the Hsod A4V Mutant
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 1n19Go back to![]() ![]()
Zinc binding site 2 out
of 2 in the Structure of the Hsod A4V Mutant
![]() Mono view ![]() Stereo pair view
Reference:
R.M.F.Cardoso,
M.M.Thayer,
M.Didonato,
T.P.Lo,
C.K.Bruns,
E.D.Getzoff,
J.A.Tainer.
Insights Into Lou Gehrig'S Disease From the Structure and Instability of the A4V Mutant of Human Cu,Zn Superoxide Dismutase. J.Mol.Biol. V. 324 247 2002.
Page generated: Wed Oct 16 17:09:18 2024
ISSN: ISSN 0022-2836 PubMed: 12441104 DOI: 10.1016/S0022-2836(02)01090-2 |
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