MolNFT v1 · #10006 · protein

Crystal structure of native vanadium-containing chloroperoxidase from curvularia inaequalis

1IDQ · Vanadium chloroperoxidase: “Crystal structure of native vanadium-containing chloroperoxidase from curvularia inaequalis”. X-ray diffraction, 1 ligand (VO4), 5 pockets (best druggability 0.77). MolNFT v1 #10006 on GenesisL1: 3D…

PDB: 1IDQ
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: 5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vanadium chloroperoxidase (EC 1.11.1.10)	protein	574	43% helix, 9% 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

5 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	1187	0.77	0.79	101	VO4
2	86	0.55	0.85	21	empty
3	127	0.40	0.75	25	empty
4	89	0.33	0.73	19	empty
5	51	0.27	0.75	13	empty

Compared structures

1IDQ · Crystal structure of native vanadium-containing chloroperoxidase from curvularia… · 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 1IDQ · PDBe 1IDQ · UniProt P49053

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