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Atomistry » Sodium » PDB 1zum-2aoc » 2ahs » |
Sodium in PDB 2ahs: Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase BetaEnzymatic activity of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta
All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta:
3.1.3.48; Protein crystallography data
The structure of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta, PDB code: 2ahs
was solved by
E.Ugochukwu,
J.Eswaran,
A.Barr,
O.Gileadi,
F.Sobott,
N.Burgess,
L.Ball,
J.Bray,
F.Von Delft,
J.Debreczeni,
G.Bunkoczi,
A.Turnbull,
S.Das,
J.Weigelt,
A.Edwards,
C.Arrowsmith,
M.Sundstrom,
S.Knapp,
Structuralgenomics Consortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2ahs:
The structure of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta
(pdb code 2ahs). 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 Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta, PDB code: 2ahs: Sodium binding site 1 out of 1 in 2ahsGo back to Sodium Binding Sites List in 2ahs
Sodium binding site 1 out
of 1 in the Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta
Mono view Stereo pair view
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.
Page generated: Tue Dec 15 05:45:19 2020
ISSN: ISSN 0092-8674 PubMed: 19167335 DOI: 10.1016/J.CELL.2008.11.038 |
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