Atomistry » Vanadium » PDB 1b8j-1yv3 » 1idu
Atomistry »
  Vanadium »
    PDB 1b8j-1yv3 »
      1idu »

Vanadium in PDB 1idu: Crystal Structure of the Peroxide Form of the Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis

Enzymatic activity of Crystal Structure of the Peroxide Form of the Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis

All present enzymatic activity of Crystal Structure of the Peroxide Form of the Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis:
1.11.1.10;

Protein crystallography data

The structure of Crystal Structure of the Peroxide Form of the Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis, PDB code: 1idu was solved by A.Messerschmidt, L.Prade, R.Wever, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.24
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 129.950, 129.950, 111.710, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / n/a

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of the Peroxide Form of the Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis (pdb code 1idu). 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 the Peroxide Form of the Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis, PDB code: 1idu:

Vanadium binding site 1 out of 1 in 1idu

Go back to Vanadium Binding Sites List in 1idu
Vanadium binding site 1 out of 1 in the Crystal Structure of the Peroxide Form of the Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis


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 the Peroxide Form of the Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1579

b:13.9
occ:1.00
V A:VO41579 0.0 13.9 1.0
O3 A:VO41579 1.6 11.4 1.0
O2 A:VO41579 1.9 18.5 1.0
O4 A:VO41579 1.9 16.1 1.0
O1 A:VO41579 1.9 14.0 1.0
NE2 A:HIS496 2.2 13.0 1.0
CE1 A:HIS496 3.1 13.0 1.0
CD2 A:HIS496 3.2 10.5 1.0
NH2 A:ARG360 3.8 16.1 1.0
NH1 A:ARG360 3.8 13.6 1.0
NH2 A:ARG490 4.0 10.5 1.0
N A:GLY403 4.0 13.5 1.0
NE A:ARG490 4.1 13.4 1.0
CE1 A:PHE397 4.1 13.9 1.0
OG A:SER402 4.2 10.5 1.0
ND1 A:HIS496 4.3 10.6 1.0
CZ A:ARG360 4.3 15.5 1.0
CG A:HIS496 4.3 9.2 1.0
O A:HOH2000 4.4 27.4 0.0
NZ A:LYS353 4.5 15.3 1.0
CZ A:ARG490 4.5 12.9 1.0
ND1 A:HIS404 4.6 8.3 1.0
CA A:SER402 4.6 7.9 1.0
N A:HIS404 4.6 14.9 1.0
CZ A:PHE397 4.7 13.2 1.0
CA A:GLY403 4.8 11.3 1.0
C A:SER402 4.8 11.4 1.0
CB A:SER402 4.9 11.6 1.0
CG A:PRO395 4.9 7.7 1.0

Reference:

A.Messerschmidt, L.Prade, R.Wever. Implications For the Catalytic Mechanism of the Vanadium-Containing Enzyme Chloroperoxidase From the Fungus Curvularia Inaequalis By X-Ray Structures of the Native and Peroxide Form. Biol.Chem. V. 378 309 1997.
ISSN: ISSN 1431-6730
PubMed: 9165086
Page generated: Wed Dec 16 02:30:05 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy