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Atomistry » Sodium » PDB 2mat-2oj0 » 2nz2 » |
Sodium in PDB 2nz2: Crystal Structure of Human Argininosuccinate Synthase in Complex with Aspartate and CitrullineEnzymatic activity of Crystal Structure of Human Argininosuccinate Synthase in Complex with Aspartate and Citrulline
All present enzymatic activity of Crystal Structure of Human Argininosuccinate Synthase in Complex with Aspartate and Citrulline:
6.3.4.5; Protein crystallography data
The structure of Crystal Structure of Human Argininosuccinate Synthase in Complex with Aspartate and Citrulline, PDB code: 2nz2
was solved by
T.Karlberg,
J.Uppenberg,
C.Arrowsmith,
H.Berglund,
R.D.Busam,
R.Collins,
A.Edwards,
U.B.Ericsson,
S.Flodin,
A.Flores,
S.Graslund,
B.M.Hallberg,
M.Hammarstrom,
M.Hogbom,
I.Johansson,
T.Kotenyova,
A.Magnusdottir,
M.Moche,
M.E.Nilsson,
P.Nordlund,
T.Nyman,
D.Ogg,
C.Persson,
J.Sagemark,
P.Stenmark,
M.Sundstrom,
A.G.Thorsell,
S.Van Den Berg,
K.Wallden,
J.Weigelt,
L.Holmberg-Schiavone,
Structural Genomics Consortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Human Argininosuccinate Synthase in Complex with Aspartate and Citrulline
(pdb code 2nz2). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Human Argininosuccinate Synthase in Complex with Aspartate and Citrulline, PDB code: 2nz2: Sodium binding site 1 out of 1 in 2nz2Go back to![]() ![]()
Sodium binding site 1 out
of 1 in the Crystal Structure of Human Argininosuccinate Synthase in Complex with Aspartate and Citrulline
![]() Mono view ![]() Stereo pair view
Reference:
T.Karlberg,
R.Collins,
S.Van Den Berg,
A.Flores,
M.Hammarstrom,
M.Hogbom,
L.Holmberg Schiavone,
J.Uppenberg.
Structure of Human Argininosuccinate Synthetase. Acta Crystallogr.,Sect.D V. 64 279 2008.
Page generated: Sun Aug 17 10:57:55 2025
ISSN: ISSN 0907-4449 PubMed: 18323623 DOI: 10.1107/S0907444907067455 |
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