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Atomistry » Arsenic » PDB 1q2o-1yhc » 1ta4 » |
Arsenic in PDB 1ta4: Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with A Bound ArsenateEnzymatic activity of Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with A Bound Arsenate
All present enzymatic activity of Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with A Bound Arsenate:
1.2.1.11; Protein crystallography data
The structure of Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with A Bound Arsenate, PDB code: 1ta4
was solved by
R.E.Viola,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Arsenic Binding Sites:
The binding sites of Arsenic atom in the Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with A Bound Arsenate
(pdb code 1ta4). This binding sites where shown within
5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with A Bound Arsenate, PDB code: 1ta4: Jump to Arsenic binding site number: 1; 2; Arsenic binding site 1 out of 2 in 1ta4Go back to Arsenic Binding Sites List in 1ta4
Arsenic binding site 1 out
of 2 in the Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with A Bound Arsenate
Mono view Stereo pair view
Arsenic binding site 2 out of 2 in 1ta4Go back to Arsenic Binding Sites List in 1ta4
Arsenic binding site 2 out
of 2 in the Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with A Bound Arsenate
Mono view Stereo pair view
Reference:
C.R.Faehnle,
J.Blanco,
R.E.Viola.
Structural Basis For Discrimination Between Oxyanion Substrates or Inhibitors in Aspartate-Beta-Semialdehyde Dehydrogenase. Acta Crystallogr.,Sect.D V. 60 2320 2004.
Page generated: Wed Jul 10 11:13:56 2024
ISSN: ISSN 0907-4449 PubMed: 15583380 DOI: 10.1107/S0907444904026411 |
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