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Atomistry » Molybdenum » PDB 1n62-2c9x » 2bih | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Molybdenum » PDB 1n62-2c9x » 2bih » |
Molybdenum in PDB 2bih: Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate ReductaseEnzymatic activity of Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase
All present enzymatic activity of Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase:
1.7.1.2; Protein crystallography data
The structure of Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase, PDB code: 2bih
was solved by
K.Fischer,
G.Barbier,
H.-J.Hecht,
R.R.Mendel,
W.H.Campbell,
G.Schwarz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Molybdenum Binding Sites:
The binding sites of Molybdenum atom in the Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase
(pdb code 2bih). This binding sites where shown within
5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase, PDB code: 2bih: Molybdenum binding site 1 out of 1 in 2bihGo back to Molybdenum Binding Sites List in 2bih
Molybdenum binding site 1 out
of 1 in the Crystal Structure of the Molybdenum-Containing Nitrate Reducing Fragment of Pichia Angusta Assimilatory Nitrate Reductase
Mono view Stereo pair view
Reference:
K.Fischer,
G.Barbier,
H.-J.Hecht,
R.R.Mendel,
W.H.Campbell,
G.Schwarz.
Structural Basis of Eukaryotic Nitrate Reduction: Crystal Structures of the Nitrate Reductase Active Site Plant Cell V. 17 1167 2005.
Page generated: Tue Dec 15 05:16:55 2020
ISSN: ISSN 1040-4651 PubMed: 15772287 DOI: 10.1105/TPC.104.029694 |
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