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Chloroperoxidase from the fungus curvularia inaequalis: mutant D292A

Analyse Chloroperoxidase from the fungus curvularia inaequalis: mutant D292A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VNE
Type: protein
Length: 574 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vanadium chloroperoxidase
EC: 1.11.1.10
UniProt: P49053
Ligands: VO4
Pockets: 4 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vanadium chloroperoxidase (EC 1.11.1.10)	protein	574	44% helix, 8% strand	P49053

Ligands and binding sites

VO4 · Vanadate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1178	0.80	0.81	99	VO4
2	93	0.56	0.86	20	empty
3	119	0.41	0.76	18	empty
4	52	0.32	0.77	14	empty

Compared structures

1VNE · Chloroperoxidase from the fungus curvularia inaequalis: mutant D292A · the same entry in another collection · chain A against A, TM-score 1.00
P49053 · AlphaFold monomer V2.0 prediction for vanadium chloroperoxidase (P49053) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P49053
Elsewhere: RCSB PDB 1VNE · PDBe 1VNE · UniProt P49053

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