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Atomistry » Zinc » PDB 1ndz-1nve » 1nj1 » |
Zinc 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:
Zinc Binding Sites:
The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Prolyl-Trna Synthetase From Methanothermobacter Thermautotrophicus Bound to Cysteine Sulfamoyl Adenylate, PDB code: 1nj1: Zinc binding site 1 out of 1 in 1nj1Go back to![]() ![]()
Zinc 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: Wed Oct 16 17:15:47 2024
ISSN: ISSN 0027-8424 PubMed: 12578991 DOI: 10.1073/PNAS.0437911100 |
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