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Atomistry » Cadmium » PDB 1mws-1qvf » 1oyr » |
Cadmium in PDB 1oyr: Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus SubtilisEnzymatic activity of Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis
All present enzymatic activity of Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis:
2.7.7.56; Protein crystallography data
The structure of Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis, PDB code: 1oyr
was solved by
L.S.Harlow,
A.Kadziola,
K.F.Jensen,
S.Larsen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Cadmium Binding Sites:
The binding sites of Cadmium atom in the Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis
(pdb code 1oyr). This binding sites where shown within
5.0 Angstroms radius around Cadmium atom.
In total 3 binding sites of Cadmium where determined in the Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis, PDB code: 1oyr: Jump to Cadmium binding site number: 1; 2; 3; Cadmium binding site 1 out of 3 in 1oyrGo back to![]() ![]()
Cadmium binding site 1 out
of 3 in the Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis
![]() Mono view ![]() Stereo pair view
Cadmium binding site 2 out of 3 in 1oyrGo back to![]() ![]()
Cadmium binding site 2 out
of 3 in the Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis
![]() Mono view ![]() Stereo pair view
Cadmium binding site 3 out of 3 in 1oyrGo back to![]() ![]()
Cadmium binding site 3 out
of 3 in the Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis
![]() Mono view ![]() Stereo pair view
Reference:
L.S.Harlow,
A.Kadziola,
K.F.Jensen,
S.Larsen.
Crystal Structure of the Phosphorolytic Exoribonuclease Rnase pH From Bacillus Subtilis and Implications For Its Quaternary Structure and Trna Binding. Protein Sci. V. 13 668 2004.
Page generated: Thu Jul 10 11:13:19 2025
ISSN: ISSN 0961-8368 PubMed: 14767080 DOI: 10.1110/PS.03477004 |
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