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Atomistry » Sodium » PDB 1w5n-1x7d » 1wnw | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 1w5n-1x7d » 1wnw » |
Sodium in PDB 1wnw: D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)Enzymatic activity of D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)
All present enzymatic activity of D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo):
1.14.99.3; Protein crystallography data
The structure of D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo), PDB code: 1wnw
was solved by
M.Unno,
T.Matsui,
M.Ikeda-Saito,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1wnw:
The structure of D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo) also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)
(pdb code 1wnw). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo), PDB code: 1wnw: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 1wnwGo back to![]() ![]()
Sodium binding site 1 out
of 2 in the D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 2 in 1wnwGo back to![]() ![]()
Sodium binding site 2 out
of 2 in the D136N Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)
![]() Mono view ![]() Stereo pair view
Reference:
T.Matsui,
M.Furukawa,
M.Unno,
T.Tomita,
M.Ikeda-Saito.
Roles of Distal Asp in Heme Oxygenase From Corynebacterium Diphtheriae, Hmuo: A Water-Driven Oxygen Activation Mechanism J.Biol.Chem. V. 280 2981 2005.
Page generated: Tue Dec 15 05:41:13 2020
ISSN: ISSN 0021-9258 PubMed: 15528205 DOI: 10.1074/JBC.M410263200 |
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