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Crystal structure of gcoa F169V bound to O-vanillin

Analyse Crystal structure of gcoa F169V bound to O-vanillin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YCP
Type
protein
Length
403 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P0DPQ7
Ligands
HEM, OKE

Structure

x-ray diffraction · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein403—P0DPQ7

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • OKE · 2-(hydroxymethyl)-6-methoxy-phenol · ligand · chains A

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

Compared structures

  • 6YCP · Crystal structure of GcoA F169V bound to o-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

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