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Vanadium in PDB 3t00: Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate

Enzymatic activity of Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate

All present enzymatic activity of Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate:
3.6.1.9;

Protein crystallography data

The structure of Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate, PDB code: 3t00 was solved by V.Agarwal, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.80
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 111.123, 111.123, 72.441, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 24.1

Other elements in 3t00:

The structure of Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate also contains other interesting chemical elements:

Nickel (Ni) 1 atom
Zinc (Zn) 2 atoms

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate (pdb code 3t00). 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 Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate, PDB code: 3t00:

Vanadium binding site 1 out of 1 in 3t00

Go back to Vanadium Binding Sites List in 3t00
Vanadium binding site 1 out of 1 in the Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V503

b:33.4
occ:1.00
V A:VO4503 0.0 33.4 1.0
O1 A:VO4503 1.9 32.2 1.0
O4 A:VO4503 1.9 32.9 1.0
O2 A:VO4503 1.9 29.3 1.0
O3 A:VO4503 1.9 31.3 1.0
OG1 A:THR68 2.0 21.2 1.0
ZN A:ZN502 3.0 30.9 1.0
CB A:THR68 3.2 20.7 1.0
ZN A:ZN501 3.3 34.0 1.0
CE1 A:HIS377 3.6 18.9 1.0
O A:HOH465 3.8 29.4 1.0
NE2 A:HIS377 3.8 19.6 1.0
N A:THR68 4.0 19.9 1.0
OD2 A:ASP211 4.0 24.1 1.0
NE2 A:HIS251 4.1 18.6 1.0
OD1 A:ASP211 4.1 21.8 1.0
CA A:THR68 4.2 20.2 1.0
CG2 A:THR68 4.2 20.4 1.0
CG A:ASP211 4.4 21.4 1.0
OD1 A:ASP29 4.7 24.6 1.0
CE1 A:HIS251 4.8 17.5 1.0
ND1 A:HIS377 4.8 20.1 1.0
NE2 A:HIS215 5.0 21.9 1.0

Reference:

V.Agarwal, S.A.Borisova, W.W.Metcalf, W.A.Van Der Donk, S.K.Nair. Structural and Mechanistic Insights Into C-P Bond Hydrolysis By Phosphonoacetate Hydrolase. Chem.Biol. V. 18 1230 2011.
ISSN: ISSN 1074-5521
PubMed: 22035792
DOI: 10.1016/J.CHEMBIOL.2011.07.019
Page generated: Thu Oct 29 07:05:15 2020

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