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Atomistry » Vanadium » PDB 1b8j-1yv3 » 1rpt » |
Vanadium in PDB 1rpt: Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction MechanismEnzymatic activity of Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction Mechanism
All present enzymatic activity of Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction Mechanism:
3.1.3.2; Protein crystallography data
The structure of Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction Mechanism, PDB code: 1rpt
was solved by
Y.Lindqvist,
G.Schneider,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Vanadium Binding Sites:
The binding sites of Vanadium atom in the Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction Mechanism
(pdb code 1rpt). This binding sites where shown within
5.0 Angstroms radius around Vanadium atom.
In total only one binding site of Vanadium was determined in the Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction Mechanism, PDB code: 1rpt: Vanadium binding site 1 out of 1 in 1rptGo back to Vanadium Binding Sites List in 1rpt
Vanadium binding site 1 out
of 1 in the Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction Mechanism
Mono view Stereo pair view
Reference:
Y.Lindqvist,
G.Schneider,
P.Vihko.
Crystal Structures of Rat Acid Phosphatase Complexed with the Transition-State Analogs Vanadate and Molybdate. Implications For the Reaction Mechanism. Eur.J.Biochem. V. 221 139 1994.
Page generated: Wed Dec 16 02:30:15 2020
ISSN: ISSN 0014-2956 PubMed: 8168503 DOI: 10.1111/J.1432-1033.1994.TB18722.X |
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