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Dehaloperoxidase B in complex with substrate O-cresol

Analyse Dehaloperoxidase B in complex with substrate O-cresol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OO1
Type: protein
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dehaloperoxidase B
UniProt: Q9NAV7
Ligands: HEM, JZ0, SO4
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dehaloperoxidase B	protein	137	75% helix, 1% strand	Q9NAV7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
JZ0 · o-cresol · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 11 copies · chains A, B

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

Pockets

3 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	255	0.68	0.83	29	HEM, JZ0
2	251	0.65	0.82	30	HEM, JZ0
3	69	0.29	0.74	23	empty

Interfaces

1 interface between chains.

A–B · 517 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6OO1 · Dehaloperoxidase B in complex with substrate o-cresol · the same entry in another collection · chain A against A, TM-score 1.00

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 Q9NAV7
Elsewhere: RCSB PDB 6OO1 · PDBe 6OO1 · UniProt Q9NAV7

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