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

Vanadium in PDB 1idq: Crystal Structure of Native Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis

Enzymatic activity of Crystal Structure of Native Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis

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

Protein crystallography data

The structure of Crystal Structure of Native Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis, PDB code: 1idq 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 / 2.03
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 131.720, 131.720, 112.460, 90.00, 90.00, 120.00
R / Rfree (%) 17 / n/a

Vanadium Binding Sites:

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

Vanadium binding site 1 out of 1 in 1idq

Go back to Vanadium Binding Sites List in 1idq
Vanadium binding site 1 out of 1 in the Crystal Structure of Native 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 Native Vanadium-Containing Chloroperoxidase From Curvularia Inaequalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1578

b:17.2
occ:1.00
V A:VO41578 0.0 17.2 1.0
O1 A:VO41578 1.6 20.8 1.0
O2 A:VO41578 1.6 15.4 1.0
O3 A:VO41578 1.6 16.1 1.0
O4 A:VO41578 1.9 17.6 1.0
NE2 A:HIS496 2.1 20.4 1.0
CD2 A:HIS496 3.0 16.3 1.0
CE1 A:HIS496 3.1 18.9 1.0
N A:GLY403 3.6 19.7 1.0
OG A:SER402 3.8 20.6 1.0
NH2 A:ARG490 4.0 14.6 1.0
NE A:ARG490 4.0 17.7 1.0
NH1 A:ARG360 4.0 20.7 1.0
ND1 A:HIS404 4.1 16.3 1.0
CA A:SER402 4.1 22.5 1.0
NH2 A:ARG360 4.1 17.5 1.0
ND1 A:HIS496 4.2 14.5 1.0
N A:HIS404 4.2 20.2 1.0
CG A:HIS496 4.2 20.6 1.0
CB A:SER402 4.2 24.2 1.0
O A:HOH1778 4.2 36.7 1.0
C A:SER402 4.3 19.3 1.0
CE1 A:PHE397 4.3 21.8 1.0
O A:HOH1911 4.4 59.1 1.0
CZ A:ARG490 4.4 11.9 1.0
NZ A:LYS353 4.5 16.0 1.0
CA A:GLY403 4.5 19.2 1.0
CZ A:ARG360 4.5 21.3 1.0
CB A:HIS404 4.8 16.5 1.0
CG A:HIS404 4.9 16.9 1.0
C A:GLY403 4.9 23.6 1.0
CG A:ARG490 4.9 21.4 1.0
CE1 A:HIS404 5.0 15.9 1.0
CZ A:PHE397 5.0 19.8 1.0
CD A:ARG490 5.0 16.3 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 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy