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Nickel 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:

Zinc (Zn) 2 atoms
Vanadium (V) 1 atom

Nickel Binding Sites:

The binding sites of Nickel 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 Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of Phosphonoacetate Hydrolase From Sinorhizobium Meliloti 1021 in Complex with Vanadate, PDB code: 3t00:

Nickel binding site 1 out of 1 in 3t00

Go back to Nickel Binding Sites List in 3t00
Nickel 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 Nickel with other atoms in the Ni 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:Ni504

b:26.6
occ:1.00
O A:HOH481 3.1 20.6 1.0
O A:HOH546 3.2 27.4 1.0
NH1 A:ARG175 3.5 17.8 1.0
N A:PHE188 3.6 13.7 1.0
CA A:PHE188 3.7 13.9 1.0
CD A:ARG175 3.7 17.5 1.0
O A:ALA184 3.7 16.1 1.0
CB A:PHE188 3.9 13.7 1.0
CG A:GLU187 4.0 14.7 1.0
O A:HOH531 4.1 28.2 1.0
CB A:GLU187 4.1 14.4 1.0
C A:GLU187 4.1 14.1 1.0
CD1 A:PHE188 4.2 17.1 1.0
O A:HOH559 4.4 31.4 1.0
CD A:GLU187 4.5 16.7 1.0
CB A:ALA184 4.5 16.2 1.0
CG A:PHE188 4.5 15.3 1.0
CZ A:ARG175 4.5 18.8 1.0
C A:ALA184 4.6 16.2 1.0
NE A:ARG175 4.6 17.7 1.0
CG A:PRO178 4.6 19.9 1.0
O A:GLU187 4.7 14.8 1.0
CA A:GLU187 4.7 14.2 1.0
CA A:ALA184 4.7 16.6 1.0
CB A:ARG175 4.7 19.0 1.0
OE1 A:GLU187 4.8 16.6 1.0
CG A:ARG175 4.8 19.0 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: Wed Dec 16 01:27:51 2020

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