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Atomistry » Chlorine » PDB 2ycm-2yj9 » 2yd3 » |
Chlorine in PDB 2yd3: Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase SigmaEnzymatic activity of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma
All present enzymatic activity of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma:
3.1.3.48; Protein crystallography data
The structure of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma, PDB code: 2yd3
was solved by
C.H.Coles,
Y.Shen,
A.P.Tenney,
C.Siebold,
G.C.Sutton,
W.Lu,
J.T.Gallagher,
E.Y.Jones,
J.G.Flanagan,
A.R.Aricescu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2yd3:
The structure of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma
(pdb code 2yd3). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma, PDB code: 2yd3: Chlorine binding site 1 out of 1 in 2yd3Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma
![]() Mono view ![]() Stereo pair view
Reference:
C.H.Coles,
Y.Shen,
A.P.Tenney,
C.Siebold,
G.C.Sutton,
W.Lu,
J.T.Gallagher,
E.Y.Jones,
J.G.Flanagan,
A.R.Aricescu.
Proteoglycan-Specific Molecular Switch For Rptp Sigma Clustering and Neuronal Extension. Science V. 332 484 2011.
Page generated: Fri Jul 11 02:35:21 2025
ISSN: ISSN 0036-8075 PubMed: 21454754 DOI: 10.1126/SCIENCE.1200840 |
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