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Vanadium in PDB 6alr: Vioc L-Arginine Hydroxylase Bound to the Vanadyl Ion, L-Arginine, and Succinate

Enzymatic activity of Vioc L-Arginine Hydroxylase Bound to the Vanadyl Ion, L-Arginine, and Succinate

All present enzymatic activity of Vioc L-Arginine Hydroxylase Bound to the Vanadyl Ion, L-Arginine, and Succinate:
1.14.11.41;

Protein crystallography data

The structure of Vioc L-Arginine Hydroxylase Bound to the Vanadyl Ion, L-Arginine, and Succinate, PDB code: 6alr was solved by A.J.Mitchell, N.P.Dunham, J.A.Bergman, A.K.Boal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.586, 67.053, 62.840, 90.00, 109.15, 90.00
R / Rfree (%) 18 / 20.6

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Vioc L-Arginine Hydroxylase Bound to the Vanadyl Ion, L-Arginine, and Succinate (pdb code 6alr). 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 Vioc L-Arginine Hydroxylase Bound to the Vanadyl Ion, L-Arginine, and Succinate, PDB code: 6alr:

Vanadium binding site 1 out of 1 in 6alr

Go back to Vanadium Binding Sites List in 6alr
Vanadium binding site 1 out of 1 in the Vioc L-Arginine Hydroxylase Bound to the Vanadyl Ion, L-Arginine, and Succinate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Vioc L-Arginine Hydroxylase Bound to the Vanadyl Ion, L-Arginine, and Succinate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V403

b:9.3
occ:1.00
V1 A:VVO403 0.0 9.3 1.0
O1 A:VVO403 1.9 11.1 1.0
OE1 A:GLU170 2.0 9.6 1.0
O4 A:SIN401 2.1 12.7 1.0
NE2 A:HIS168 2.2 8.7 1.0
NE2 A:HIS316 2.3 8.7 1.0
O3 A:SIN401 2.3 14.2 1.0
C4 A:SIN401 2.6 13.2 1.0
CD A:GLU170 3.0 9.7 1.0
CE1 A:HIS168 3.1 8.7 1.0
CE1 A:HIS316 3.2 8.6 1.0
CD2 A:HIS316 3.3 8.6 1.0
OE2 A:GLU170 3.3 10.4 1.0
CD2 A:HIS168 3.3 8.7 1.0
NH1 A:ARG334 4.1 12.9 1.0
C3 A:SIN401 4.1 13.1 1.0
N A:ARG402 4.1 16.5 1.0
ND1 A:HIS168 4.3 8.6 1.0
ND1 A:HIS316 4.3 8.7 1.0
CG A:HIS316 4.3 8.5 1.0
CG A:GLU170 4.4 9.4 1.0
CG A:HIS168 4.4 8.6 1.0
CB A:ARG402 4.6 16.2 1.0
CG A:ARG402 4.6 16.1 1.0
CB A:GLU170 4.7 9.2 1.0
C2 A:SIN401 4.9 12.7 1.0
CD2 A:LEU165 4.9 9.6 1.0
CA A:ARG402 4.9 16.1 1.0

Reference:

A.J.Mitchell, N.P.Dunham, R.J.Martinie, J.A.Bergman, C.J.Pollock, K.Hu, B.D.Allen, W.C.Chang, A.Silakov, J.M.Bollinger, C.Krebs, A.K.Boal. Visualizing the Reaction Cycle in An Iron(II)- and 2-(Oxo)-Glutarate-Dependent Hydroxylase. J. Am. Chem. Soc. V. 139 13830 2017.
ISSN: ESSN 1520-5126
PubMed: 28823155
DOI: 10.1021/JACS.7B07374
Page generated: Thu Oct 29 07:05:58 2020

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