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Sodium in PDB 1wnx: D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)

Enzymatic activity of D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)

All present enzymatic activity of D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo):
1.14.99.3;

Protein crystallography data

The structure of D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo), PDB code: 1wnx 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:

Resolution Low / High (Å) 40.00 / 1.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 106.151, 63.722, 79.296, 90.00, 130.28, 90.00
R / Rfree (%) 15 / 20.1

Other elements in 1wnx:

The structure of D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo) also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo) (pdb code 1wnx). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo), PDB code: 1wnx:

Sodium binding site 1 out of 1 in 1wnx

Go back to Sodium Binding Sites List in 1wnx
Sodium binding site 1 out of 1 in the D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of D136E Mutant of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na3001

b:26.6
occ:1.00
OE2 A:GLU115 2.2 41.8 1.0
CD A:GLU115 3.1 33.3 1.0
CG A:GLU115 3.7 27.1 1.0
OE1 A:GLU115 4.0 38.2 1.0
O A:HOH3123 4.1 37.7 1.0
CB A:GLU115 4.6 21.2 1.0

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.
ISSN: ISSN 0021-9258
PubMed: 15528205
DOI: 10.1074/JBC.M410263200
Page generated: Tue Dec 15 05:41:13 2020

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