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Crystal structure of the ORF6* (CYP165D3) monooxygenase involved in teicoplanin biosynthesis

Analyse Crystal structure of the ORF6* (CYP165D3) monooxygenase involved in teicoplanin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OO3
Type
protein
Length
371 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Oxy protein
UniProt
Q6ZZI7
Ligands
HEM
Pockets
4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOxy proteinprotein37157% helix, 10% strandQ6ZZI7

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17080.790.8369HEM
2880.430.7919empty
31060.410.7719empty
4670.340.7616empty

Compared structures

  • 3OO3 · Crystal Structure of the Orf6* (CYP165D3) Monooxygenase Involved in Teicoplanin… · the same entry in another collection · chain A against A, TM-score 1.00

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