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Atomistry » Magnesium » PDB 1ngj-1nn5 » 1nj6 » |
Magnesium in PDB 1nj6: Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl AdenylateEnzymatic activity of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate
All present enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate:
6.1.1.15; Protein crystallography data
The structure of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine Sulfamoyl Adenylate, PDB code: 1nj6
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 1nj6:
The structure of Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine 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 Alanine Sulfamoyl Adenylate
(pdb code 1nj6). 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 Alanine Sulfamoyl Adenylate, PDB code: 1nj6: Magnesium binding site 1 out of 1 in 1nj6Go back to Magnesium Binding Sites List in 1nj6
Magnesium binding site 1 out
of 1 in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Alanine 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: Mon Dec 14 06:32:51 2020
ISSN: ISSN 0027-8424 PubMed: 12578991 DOI: 10.1073/PNAS.0437911100 |
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