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Sodium in PDB 1uuo: Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar

Enzymatic activity of Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar

All present enzymatic activity of Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar:
1.3.99.11;

Protein crystallography data

The structure of Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar, PDB code: 1uuo was solved by M.Hansen, J.Le Nours, E.Johansson, T.Antal, A.Ullrich, M.Loffler, S.Larsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.44
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 49.753, 95.801, 144.469, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 26.3

Other elements in 1uuo:

The structure of Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar also contains other interesting chemical elements:

Fluorine (F) 2 atoms
Nickel (Ni) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar (pdb code 1uuo). 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 Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar, PDB code: 1uuo:

Sodium binding site 1 out of 1 in 1uuo

Go back to Sodium Binding Sites List in 1uuo
Sodium binding site 1 out of 1 in the Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Rat Dihydroorotate Dehydrogenase (Dhod)in Complex with Brequinar within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1401

b:66.1
occ:1.00
CB A:ARG318 4.8 23.6 1.0
CE1 A:HIS394 4.9 42.7 1.0
ND1 A:HIS394 4.9 42.0 1.0

Reference:

M.Hansen, J.Le Nours, E.Johansson, T.Antal, A.Ullrich, M.Loffler, S.Larsen. Inhibitor Binding in A Class 2 Dihydroorotate Dehydrogenase Causes Variations in the Membrane-Associated N-Terminal Domain Protein Sci. V. 13 1031 2004.
ISSN: ISSN 0961-8368
PubMed: 15044733
DOI: 10.1110/PS.03533004
Page generated: Tue Dec 15 05:37:02 2020

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