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Atomistry » Chlorine » PDB 2hr2-2i5x » 2i4g | |||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2hr2-2i5x » 2i4g » |
Chlorine in PDB 2i4g: Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with A Sulfamic Acid (Soaking Experiment)Enzymatic activity of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with A Sulfamic Acid (Soaking Experiment)
All present enzymatic activity of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with A Sulfamic Acid (Soaking Experiment):
3.1.3.48; Protein crystallography data
The structure of Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with A Sulfamic Acid (Soaking Experiment), PDB code: 2i4g
was solved by
A.G.Evdokimov,
M.E.Pokross,
R.L.Walter,
M.Mekel,
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 Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with A Sulfamic Acid (Soaking Experiment)
(pdb code 2i4g). 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 Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with A Sulfamic Acid (Soaking Experiment), PDB code: 2i4g: Chlorine binding site 1 out of 1 in 2i4gGo back to Chlorine Binding Sites List in 2i4g
Chlorine binding site 1 out
of 1 in the Structural Studies of Protein Tyrosine Phosphatase Beta Catalytic Domain in Complex with A Sulfamic Acid (Soaking Experiment)
Mono view Stereo pair view
Reference:
A.G.Evdokimov,
M.Pokross,
R.Walter,
M.Mekel,
B.Cox,
C.Li,
R.Bechard,
F.Genbauffe,
R.Andrews,
C.Diven,
B.Howard,
V.Rastogi,
J.Gray,
M.Maier,
K.G.Peters.
Engineering the Catalytic Domain of Human Protein Tyrosine Phosphatase Beta For Structure-Based Drug Discovery. Acta Crystallogr.,Sect.D V. 62 1435 2006.
Page generated: Sat Dec 12 09:08:05 2020
ISSN: ISSN 0907-4449 PubMed: 17139078 DOI: 10.1107/S0907444906037784 |
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