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Atomistry » Magnesium » PDB 1nzz-1oev » 1o6b » |
Magnesium in PDB 1o6b: Crystal Structure of Phosphopantetheine Adenylyltransferase with AdpEnzymatic activity of Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp
All present enzymatic activity of Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp:
2.7.7.3; Protein crystallography data
The structure of Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp, PDB code: 1o6b
was solved by
Structural Genomix,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1o6b:
The structure of Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp
(pdb code 1o6b). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp, PDB code: 1o6b: Magnesium binding site 1 out of 1 in 1o6bGo back to Magnesium Binding Sites List in 1o6b
Magnesium binding site 1 out
of 1 in the Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp
Mono view Stereo pair view
Reference:
J.Badger,
J.M.Sauder,
J.M.Adams,
S.Antonysamy,
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M.D.Buchanan,
Y.Batiyenko,
J.A.Christopher,
S.Emtage,
A.Eroshkina,
I.Feil,
E.B.Furlong,
K.S.Gajiwala,
X.Gao,
D.He,
J.Hendle,
A.Huber,
K.Hoda,
P.Kearins,
C.Kissinger,
B.Laubert,
H.A.Lewis,
J.Lin,
K.Loomis,
D.Lorimer,
G.Louie,
M.Maletic,
C.D.Marsh,
I.Miller,
J.Molinari,
H.J.Muller-Dieckmann,
J.M.Newman,
B.W.Noland,
B.Pagarigan,
F.Park,
T.S.Peat,
K.W.Post,
S.Radojicic,
A.Ramos,
R.Romero,
M.E.Rutter,
W.E.Sanderson,
K.D.Schwinn,
J.Tresser,
J.Winhoven,
T.A.Wright,
L.Wu,
J.Xu,
T.J.Harris.
Structural Analysis of A Set of Proteins Resulting From A Bacterial Genomics Project Proteins V. 60 787 2005.
Page generated: Mon Dec 14 06:34:20 2020
ISSN: ISSN 0887-3585 PubMed: 16021622 DOI: 10.1002/PROT.20541 |
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