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Atomistry » Chlorine » PDB 2ycm-2yj9 » 2yd6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2ycm-2yj9 » 2yd6 » |
Chlorine in PDB 2yd6: Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase DeltaEnzymatic activity of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Delta
All present enzymatic activity of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Delta:
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 Delta, PDB code: 2yd6
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:
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 Delta
(pdb code 2yd6). 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 Delta, PDB code: 2yd6: Chlorine binding site 1 out of 1 in 2yd6Go 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 Delta
![]() 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: Sat Jul 20 14:58:10 2024
ISSN: ISSN 0036-8075 PubMed: 21454754 DOI: 10.1126/SCIENCE.1200840 |
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