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Direct-evolutioned unspecific peroxygenase from agrocybe aegerita, in complex with veratryl alcohol

Analyse Direct-evolutioned unspecific peroxygenase from agrocybe aegerita, in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EL4
Type
protein
Length
326 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
B9W4V6
Ligands
HEM, VOH, NAG, MG, CL, PO4

Structure

x-ray diffraction · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein326—B9W4V6

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • VOH · Veratryl alcohol · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
  • MG · Magnesium ion · metal · chains A
  • CL · Chloride ion · ion · chains A
  • PO4 · Phosphate ion · ion · chains A
  • GOL · Glycerol · additive · 5 copies · chains A

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

Compared structures

  • 6EL4 · Direct-evolutioned unspecific peroxygenase from Agrocybe aegerita, in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • B9W4V6 · AlphaFold monomer V2.0 prediction for aromatic peroxygenase (B9W4V6) · a predicted model of the same protein · chain A against A, TM-score 1.00

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