Sodium in PDB 2ooq: Crystal Structure of the Human Receptor Phosphatase Ptprt

All present enzymatic activity of Crystal Structure of the Human Receptor Phosphatase Ptprt:
3.1.3.48;

The structure of Crystal Structure of the Human Receptor Phosphatase Ptprt, PDB code: 2ooq was solved by E.Ugochukwu, I.Alfano, A.Barr, T.Keates, J.Eswaran, E.Salah, P.Savitsky, G.Bunkoczi, A.Edwards, C.H.Arrowsmith, J.Weigelt, M.Sundstrom, F.Vondelft, S.Knapp, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	89.77 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.186, 86.697, 91.120, 90.00, 99.89, 90.00
R / Rfree (%)	14.5 / 18.8

The binding sites of Sodium atom in the Crystal Structure of the Human Receptor Phosphatase Ptprt (pdb code 2ooq). 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 Human Receptor Phosphatase Ptprt, PDB code: 2ooq:

Sodium binding site 1 out of 1 in the Crystal Structure of the Human Receptor Phosphatase Ptprt


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 Human Receptor Phosphatase Ptprt within 5.0Å range: probe atom residue distance (Å) B Occ B:Na501 b:49.7 occ:1.00 NE2 B:HIS978 3.0 32.2 1.0 OD2 B:ASP1120 3.2 27.9 1.0 CD1 B:ILE1102 3.4 30.8 1.0 O B:HOH1364 3.8 25.4 1.0 CE1 B:HIS978 3.9 48.1 1.0 O B:HOH1313 3.9 42.3 1.0 CD2 B:HIS978 4.0 31.9 1.0 CG B:ASP1120 4.0 26.2 1.0 OD1 B:ASP1120 4.0 27.4 1.0 CG B:LYS1092 4.5 30.5 1.0 OH B:TYR979 4.7 28.9 1.0 CE1 B:TYR979 4.7 25.8 1.0 CA B:LYS1092 4.8 24.0 1.0 NZ B:LYS1092 4.9 41.8 1.0 CG1 B:ILE1102 4.9 25.5 1.0 CG1 B:VAL1091 4.9 20.7 1.0

A.J.Barr, E.Ugochukwu, W.H.Lee, O.N.King, P.Filippakopoulos, I.Alfano, P.Savitsky, N.A.Burgess-Brown, S.Muller, S.Knapp. Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome. Cell(Cambridge,Mass.) V. 136 352 2009.
ISSN: ISSN 0092-8674
PubMed: 19167335
DOI: 10.1016/J.CELL.2008.11.038