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Atomistry » Cadmium » PDB 1jv4-1mwr » 1lxt | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cadmium » PDB 1jv4-1mwr » 1lxt » |
Cadmium in PDB 1lxt: Structure of Phosphotransferase Phosphoglucomutase From RabbitEnzymatic activity of Structure of Phosphotransferase Phosphoglucomutase From Rabbit
All present enzymatic activity of Structure of Phosphotransferase Phosphoglucomutase From Rabbit:
5.4.2.2; Protein crystallography data
The structure of Structure of Phosphotransferase Phosphoglucomutase From Rabbit, PDB code: 1lxt
was solved by
W.J.Ray Junior,
S.Baranidharan,
Y.Liu,
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 Structure of Phosphotransferase Phosphoglucomutase From Rabbit
(pdb code 1lxt). This binding sites where shown within
5.0 Angstroms radius around Cadmium atom.
In total 2 binding sites of Cadmium where determined in the Structure of Phosphotransferase Phosphoglucomutase From Rabbit, PDB code: 1lxt: Jump to Cadmium binding site number: 1; 2; Cadmium binding site 1 out of 2 in 1lxtGo back to Cadmium Binding Sites List in 1lxt
Cadmium binding site 1 out
of 2 in the Structure of Phosphotransferase Phosphoglucomutase From Rabbit
Mono view Stereo pair view
Cadmium binding site 2 out of 2 in 1lxtGo back to Cadmium Binding Sites List in 1lxt
Cadmium binding site 2 out
of 2 in the Structure of Phosphotransferase Phosphoglucomutase From Rabbit
Mono view Stereo pair view
Reference:
Y.Liu,
W.J.Ray,
S.Baranidharan.
Structure of Rabbit Muscle Phosphoglucomutase Refined at 2.4 A Resolution. Acta Crystallogr.,Sect.D V. 53 392 1997.
Page generated: Sat Dec 12 08:10:51 2020
ISSN: ISSN 0907-4449 PubMed: 15299905 DOI: 10.1107/S0907444997000875 |
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