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Atomistry » Magnesium » PDB 101d-1an0 » 1aih » |
Magnesium in PDB 1aih: Catalytic Domain of Bacteriophage HP1 IntegraseProtein crystallography data
The structure of Catalytic Domain of Bacteriophage HP1 Integrase, PDB code: 1aih
was solved by
A.B.Hickman,
S.Waninger,
J.J.Scocca,
F.Dyda,
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 Catalytic Domain of Bacteriophage HP1 Integrase
(pdb code 1aih). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Catalytic Domain of Bacteriophage HP1 Integrase, PDB code: 1aih: Jump to Magnesium binding site number: 1; 2; 3; 4; 5; Magnesium binding site 1 out of 5 in 1aihGo back to Magnesium Binding Sites List in 1aih
Magnesium binding site 1 out
of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase
Mono view Stereo pair view
Magnesium binding site 2 out of 5 in 1aihGo back to Magnesium Binding Sites List in 1aih
Magnesium binding site 2 out
of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase
Mono view Stereo pair view
Magnesium binding site 3 out of 5 in 1aihGo back to Magnesium Binding Sites List in 1aih
Magnesium binding site 3 out
of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase
Mono view Stereo pair view
Magnesium binding site 4 out of 5 in 1aihGo back to Magnesium Binding Sites List in 1aih
Magnesium binding site 4 out
of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase
Mono view Stereo pair view
Magnesium binding site 5 out of 5 in 1aihGo back to Magnesium Binding Sites List in 1aih
Magnesium binding site 5 out
of 5 in the Catalytic Domain of Bacteriophage HP1 Integrase
Mono view Stereo pair view
Reference:
A.B.Hickman,
S.Waninger,
J.J.Scocca,
F.Dyda.
Molecular Organization in Site-Specific Recombination: the Catalytic Domain of Bacteriophage HP1 Integrase at 2.7 A Resolution. Cell(Cambridge,Mass.) V. 89 227 1997.
Page generated: Tue Aug 13 02:03:38 2024
ISSN: ISSN 0092-8674 PubMed: 9108478 DOI: 10.1016/S0092-8674(00)80202-0 |
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