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Atomistry » Chlorine » PDB 2j6w-2jh6 » 2j7t | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2j6w-2jh6 » 2j7t » |
Chlorine in PDB 2j7t: Crystal Structure of Human Serine Threonine Kinase-10 Bound to SU11274Enzymatic activity of Crystal Structure of Human Serine Threonine Kinase-10 Bound to SU11274
All present enzymatic activity of Crystal Structure of Human Serine Threonine Kinase-10 Bound to SU11274:
2.7.11.1; Protein crystallography data
The structure of Crystal Structure of Human Serine Threonine Kinase-10 Bound to SU11274, PDB code: 2j7t
was solved by
A.C.W.Pike,
P.Rellos,
O.Fedorov,
S.Das,
J.Debreczeni,
F.Sobott,
S.Watt,
P.Savitsky,
J.Eswaran,
A.P.Turnbull,
E.Papagrigoriou,
E.Ugochukwa,
F.Gorrec,
C.C.Umeano,
F.Von Delft,
C.H.Arrowsmith,
A.Edwards,
J.Weigelt,
M.Sundstrom,
S.Knapp,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2j7t:
The structure of Crystal Structure of Human Serine Threonine Kinase-10 Bound to SU11274 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Human Serine Threonine Kinase-10 Bound to SU11274
(pdb code 2j7t). 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 Human Serine Threonine Kinase-10 Bound to SU11274, PDB code: 2j7t: Chlorine binding site 1 out of 1 in 2j7tGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of Human Serine Threonine Kinase-10 Bound to SU11274
![]() Mono view ![]() Stereo pair view
Reference:
A.C.W.Pike,
P.Rellos,
F.H.Niesen,
A.Turnbull,
A.W.Oliver,
S.A.Parker,
B.E.Turk,
L.H.Pearl,
S.Knapp.
Activation Segment Dimerization: A Mechanism For Kinase Autophosphorylation of Non-Consensus Sites. Embo J. V. 27 704 2008.
Page generated: Sat Jul 20 08:44:09 2024
ISSN: ISSN 0261-4189 PubMed: 18239682 DOI: 10.1038/EMBOJ.2008.8 |
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