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Vanadium in PDB 1rpt: Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction Mechanism

Enzymatic 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:

Resolution Low / High (Å) N/A / 3.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.400, 89.400, 152.000, 90.00, 90.00, 120.00
R / Rfree (%) 21.5 / n/a

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 1rpt

Go 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

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structures of Rat Acid Phosphatase Complexed with the Transitions State Analogs Vanadate and Molybdate: Implications For the Reaction Mechanism within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V343

b:16.3
occ:1.00
V A:VO4343 0.0 16.3 1.0
O2 A:VO4343 1.5 16.3 1.0
O1 A:VO4343 1.7 16.3 1.0
O4 A:VO4343 1.7 16.3 1.0
O3 A:VO4343 1.8 16.3 1.0
NE2 A:HIS12 2.0 16.3 1.0
CD2 A:HIS12 2.9 16.3 1.0
CE1 A:HIS12 2.9 16.3 1.0
ND1 A:HIS257 3.6 16.3 1.0
NH1 A:ARG79 3.7 16.3 1.0
NE A:ARG15 3.9 16.3 1.0
NH1 A:ARG11 3.9 16.3 1.0
OD2 A:ASP258 3.9 16.3 1.0
ND1 A:HIS12 4.0 16.3 1.0
CG A:HIS12 4.0 16.3 1.0
NH2 A:ARG15 4.1 16.3 1.0
CZ A:ARG15 4.3 16.3 1.0
N A:ASP258 4.4 16.3 1.0
CG A:HIS257 4.5 16.3 1.0
CG A:ASP258 4.5 16.3 1.0
CZ A:ARG79 4.5 16.3 1.0
CE1 A:HIS257 4.6 16.3 1.0
CZ A:ARG11 4.6 16.3 1.0
CB A:HIS257 4.6 16.3 1.0
CA A:HIS257 4.7 16.3 1.0
CD A:ARG15 4.8 16.3 1.0
CD A:ARG79 4.9 16.3 1.0

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.
ISSN: ISSN 0014-2956
PubMed: 8168503
DOI: 10.1111/J.1432-1033.1994.TB18722.X
Page generated: Thu Oct 29 07:04:24 2020

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