Sodium in PDB 8vr2: Crystal Structure of the PCRYO_0617 Oxidoreductase/Decarboxylase From Psychrobacter Cryohalolentis K5 in the Presence of Nad and Udp

The structure of Crystal Structure of the PCRYO_0617 Oxidoreductase/Decarboxylase From Psychrobacter Cryohalolentis K5 in the Presence of Nad and Udp, PDB code: 8vr2 was solved by N.J.Bockhaus, J.B.Thoden, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.95 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.579, 114.849, 206.045, 90, 90, 90
R / Rfree (%)	19.6 / 24.1

The binding sites of Sodium atom in the Crystal Structure of the PCRYO_0617 Oxidoreductase/Decarboxylase From Psychrobacter Cryohalolentis K5 in the Presence of Nad and Udp (pdb code 8vr2). 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 Crystal Structure of the PCRYO_0617 Oxidoreductase/Decarboxylase From Psychrobacter Cryohalolentis K5 in the Presence of Nad and Udp, PDB code: 8vr2:

Sodium binding site 1 out of 1 in the Crystal Structure of the PCRYO_0617 Oxidoreductase/Decarboxylase From Psychrobacter Cryohalolentis K5 in the Presence of Nad and Udp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the PCRYO_0617 Oxidoreductase/Decarboxylase From Psychrobacter Cryohalolentis K5 in the Presence of Nad and Udp within 5.0Å range: probe atom residue distance (Å) B Occ D:Na403 b:38.1 occ:1.00 O D:HOH518 2.4 33.1 1.0 O D:HOH620 2.5 37.3 1.0 O D:HOH581 2.6 28.6 1.0 O D:HOH589 2.6 35.9 1.0 O D:HOH631 3.9 32.3 1.0 ND2 D:ASN37 3.9 34.5 1.0 ND2 D:ASN60 4.0 34.0 1.0 O D:HOH559 4.4 30.2 1.0 NH2 D:ARG95 4.4 28.4 1.0 O D:HOH601 4.5 37.9 1.0 OE2 D:GLU39 4.5 29.6 1.0

N.J.Bockhaus, M.M.Dunsirn, J.B.Thoden, H.M.Holden. Biochemical Investigation of the Enzymes Required For the Production of 2,3,4-Triacetoamido-2,3,4-Trideoxy-L-Arabinose in Psychrobacter Cryohalolentis K5 To Be Published.