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 / R_free (%)*	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

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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

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