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Atomistry » Chlorine » PDB 3mvu-3n4a » 3n0p | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 3mvu-3n4a » 3n0p » |
Chlorine in PDB 3n0p: A Mutant Human Prolactin Receptor Antagonist H30A in Complex with the Extracellular Domain of the Human Prolactin ReceptorProtein crystallography data
The structure of A Mutant Human Prolactin Receptor Antagonist H30A in Complex with the Extracellular Domain of the Human Prolactin Receptor, PDB code: 3n0p
was solved by
M.V.Kulkarni,
M.C.Tettamanzi,
J.W.Murphy,
C.Keeler,
D.G.Myszka,
N.E.Chayen,
E.J.Lolis,
M.E.Hodsdon,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3n0p:
The structure of A Mutant Human Prolactin Receptor Antagonist H30A in Complex with the Extracellular Domain of the Human Prolactin Receptor also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the A Mutant Human Prolactin Receptor Antagonist H30A in Complex with the Extracellular Domain of the Human Prolactin Receptor
(pdb code 3n0p). 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 A Mutant Human Prolactin Receptor Antagonist H30A in Complex with the Extracellular Domain of the Human Prolactin Receptor, PDB code: 3n0p: Chlorine binding site 1 out of 1 in 3n0pGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the A Mutant Human Prolactin Receptor Antagonist H30A in Complex with the Extracellular Domain of the Human Prolactin Receptor
![]() Mono view ![]() Stereo pair view
Reference:
M.V.Kulkarni,
M.C.Tettamanzi,
J.W.Murphy,
C.Keeler,
D.G.Myszka,
N.E.Chayen,
E.J.Lolis,
M.E.Hodsdon.
Two Independent Histidines, One in Human Prolactin and One in Its Receptor, Are Critical For pH-Dependent Receptor Recognition and Activation. J.Biol.Chem. V. 285 38524 2010.
Page generated: Fri Jul 11 08:03:35 2025
ISSN: ISSN 0021-9258 PubMed: 20889499 DOI: 10.1074/JBC.M110.172072 |
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