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Atomistry » Magnesium » PDB 2fl6-2fwq » 2fna » |
Magnesium in PDB 2fna: Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A ResolutionProtein crystallography data
The structure of Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution, PDB code: 2fna
was solved by
Joint Center For Structural Genomics (Jcsg),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution
(pdb code 2fna). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution, PDB code: 2fna: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 2fnaGo back to Magnesium Binding Sites List in 2fna
Magnesium binding site 1 out
of 2 in the Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 2fnaGo back to Magnesium Binding Sites List in 2fna
Magnesium binding site 2 out
of 2 in the Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution
Mono view Stereo pair view
Reference:
Q.Xu,
C.L.Rife,
D.Carlton,
M.D.Miller,
S.S.Krishna,
M.A.Elsliger,
P.Abdubek,
T.Astakhova,
H.J.Chiu,
T.Clayton,
L.Duan,
J.Feuerhelm,
S.K.Grzechnik,
J.Hale,
G.W.Han,
L.Jaroszewski,
K.K.Jin,
H.E.Klock,
M.W.Knuth,
A.Kumar,
D.Mcmullan,
A.T.Morse,
E.Nigoghossian,
L.Okach,
S.Oommachen,
J.Paulsen,
R.Reyes,
H.Van Den Bedem,
K.O.Hodgson,
J.Wooley,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
I.A.Wilson.
Crystal Structure of A Novel Archaeal Aaa+ Atpase SSO1545 From Sulfolobus Solfataricus. Proteins V. 74 1041 2009.
Page generated: Tue Aug 13 23:15:35 2024
ISSN: ISSN 0887-3585 PubMed: 19089981 DOI: 10.1002/PROT.22325 |
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