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Atomistry » Chlorine » PDB 3bga-3bpr » 3blj » |
Chlorine in PDB 3blj: Crystal Structure of Human Poly(Adp-Ribose) Polymerase 15, Catalytic FragmentEnzymatic activity of Crystal Structure of Human Poly(Adp-Ribose) Polymerase 15, Catalytic Fragment
All present enzymatic activity of Crystal Structure of Human Poly(Adp-Ribose) Polymerase 15, Catalytic Fragment:
2.4.2.30; Protein crystallography data
The structure of Crystal Structure of Human Poly(Adp-Ribose) Polymerase 15, Catalytic Fragment, PDB code: 3blj
was solved by
T.Karlberg,
L.Lehtio,
C.H.Arrowsmith,
H.Berglund,
R.D.Busam,
R.Collins,
L.G.Dahlgren,
A.M.Edwards,
S.Flodin,
A.Flores,
S.Graslund,
M.Hammarstrom,
I.Johansson,
A.Kallas,
T.Kotenyova,
M.Moche,
M.E.Nilsson,
P.Nordlund,
T.Nyman,
C.Persson,
J.Sagemark,
L.Svensson,
A.G.Thorsell,
L.Tresaugues,
S.Van Den Berg,
M.Welin,
J.Weigelt,
Structural Genomics Consortium(Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3blj:
The structure of Crystal Structure of Human Poly(Adp-Ribose) Polymerase 15, Catalytic Fragment also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Human Poly(Adp-Ribose) Polymerase 15, Catalytic Fragment
(pdb code 3blj). 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 Poly(Adp-Ribose) Polymerase 15, Catalytic Fragment, PDB code: 3blj: Chlorine binding site 1 out of 1 in 3bljGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of Human Poly(Adp-Ribose) Polymerase 15, Catalytic Fragment
![]() Mono view ![]() Stereo pair view
Reference:
T.Karlberg,
M.Klepsch,
A.G.Thorsell,
C.D.Andersson,
A.Linusson,
H.Schuler.
Structural Basis For Lack of Adp-Ribosyltransferase Activity in Poly(Adp-Ribose) Polymerase-13/Zinc Finger Antiviral Protein. J.Biol.Chem. V. 290 7336 2015.
Page generated: Fri Jul 11 03:29:20 2025
ISSN: ISSN 0021-9258 PubMed: 25635049 DOI: 10.1074/JBC.M114.630160 |
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