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Atomistry » Magnesium » PDB 1ngj-1nn5 » 1nj1 » |
Magnesium in PDB 1nj1: Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl AdenylateEnzymatic activity of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl Adenylate
All present enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl Adenylate:
6.1.1.15; Protein crystallography data
The structure of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl Adenylate, PDB code: 1nj1
was solved by
S.Kamtekar,
W.D.Kennedy,
J.Wang,
C.Stathopoulos,
D.Soll,
T.A.Steitz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1nj1:
The structure of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl Adenylate also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl Adenylate
(pdb code 1nj1). 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 Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl Adenylate, PDB code: 1nj1: Magnesium binding site 1 out of 1 in 1nj1Go back to Magnesium Binding Sites List in 1nj1
Magnesium binding site 1 out
of 1 in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl Adenylate
Mono view Stereo pair view
Reference:
S.Kamtekar,
W.D.Kennedy,
J.Wang,
C.Stathopoulos,
D.Soll,
T.A.Steitz.
The Structural Basis of Cysteine Aminoacylation of Trnapro By Prolyl-Trna Synthetases Proc.Natl.Acad.Sci.Usa V. 100 1673 2003.
Page generated: Tue Aug 13 10:04:17 2024
ISSN: ISSN 0027-8424 PubMed: 12578991 DOI: 10.1073/PNAS.0437911100 |
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