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Sodium in PDB 2h4v: Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma

Enzymatic activity of Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma

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

Protein crystallography data

The structure of Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma, PDB code: 2h4v was solved by E.Ugochukwu, A.Barr, S.Das, J.Eswaran, P.Savitsky, M.Sundstrom, A.Edwards, C.Arrowsmith, J.Weigelt, J.Debreczeni, F.Von Delft, S.Knapp, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.23 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.849, 78.859, 121.758, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 18.1

Other elements in 2h4v:

The structure of Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma also contains other interesting chemical elements:

Chlorine (Cl) 7 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma (pdb code 2h4v). 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 Tyrosine Receptor Phosphatase Gamma, PDB code: 2h4v:

Sodium binding site 1 out of 1 in 2h4v

Go back to Sodium Binding Sites List in 2h4v
Sodium binding site 1 out of 1 in the Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma


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 Tyrosine Receptor Phosphatase Gamma within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1130

b:24.5
occ:1.00
 O B:TYR1023 2.7 15.6 1.0
O B:HOH52 2.7 20.2 1.0
N B:TRP1026 3.0 18.3 1.0
CB B:TRP1026 3.3 17.5 1.0
C B:THR1024 3.4 18.5 1.0
C B:TYR1023 3.4 16.4 1.0
N B:GLN1025 3.4 16.6 1.0
CA B:THR1024 3.5 15.7 1.0
CA B:TRP1026 3.7 18.6 1.0
N B:THR1024 3.7 15.8 1.0
O B:THR1024 3.9 18.8 1.0
CD2 B:TYR1023 3.9 17.4 1.0
CA B:THR951 3.9 17.6 1.0
C B:THR951 3.9 19.8 1.0
O B:TRP1026 4.0 21.3 1.0
C B:GLN1025 4.0 21.0 1.0
N B:THR951 4.0 17.6 1.0
ND2 B:ASN952 4.0 20.9 1.0
N B:ASN952 4.0 15.9 1.0
CA B:GLN1025 4.2 16.6 1.0
C B:ILE950 4.3 15.5 1.0
C B:TRP1026 4.3 20.9 1.0
OE2 B:GLU955 4.3 17.4 1.0
CG B:ASN952 4.4 19.8 1.0
O B:THR951 4.4 17.6 1.0
NH1 B:ARG1066 4.5 18.1 1.0
O B:ILE950 4.6 18.1 1.0
CB B:TYR1023 4.6 15.7 1.0
CA B:TYR1023 4.6 16.2 1.0
CG B:TYR1023 4.7 14.4 1.0
CG B:TRP1026 4.7 20.5 1.0
CE2 B:TYR1023 4.7 19.3 1.0
OD1 B:ASN952 4.8 25.4 1.0
CB B:THR1024 5.0 15.0 1.0

Reference:

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
Page generated: Mon Oct 7 02:43:48 2024

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