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Crystal structure of gcoa T296G bound to P-vanillin

Analyse Crystal structure of gcoa T296G bound to P-vanillin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6YCL
Type: protein
Length: 403 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aromatic O-demethylase, cytochrome P450 subunit
EC: 1.14.14.-
UniProt: P0DPQ7
Ligands: V55, HEM
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aromatic O-demethylase, cytochrome P450 subunit (EC 1.14.14.-)	protein	403	56% helix, 11% strand	P0DPQ7

Ligands and binding sites

V55 · 4-hydroxy-3-methoxybenzaldehyde · ligand · chains A
HEM · Protoporphyrin IX containing Fe · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	422	0.86	0.94	48	V55, HEM
2	92	0.38	0.76	15	empty

Compared structures

6YCL · Crystal structure of GcoA T296G bound to p-vanillin · the same entry in another collection · chain A against A, TM-score 1.00
P0DPQ7 · AlphaFold monomer V2.0 prediction for aromatic O-demethylase, cytochrome P450 subunit… · a predicted model of the same protein · 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 P0DPQ7
Elsewhere: RCSB PDB 6YCL · PDBe 6YCL · UniProt P0DPQ7

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