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1LFK

Crystal structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction During Vancomycin Biosynthesis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0033072biological_processvancomycin biosynthetic process
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 430
ChainResidue
AMET55
AGLY237
AASN240
APRO283
APRO286
ATHR287
AARG289
AALA339
APHE340
AGLY341
AHIS345
ALEU88
ACYS347
AHOH448
AHOH698
AMET89
AHIS96
AARG100
APHE107
ALEU152
ALEU155
AALA236

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGVHHCLG
ChainResidueDetails
APHE340-GLY349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS347

218853

PDB entries from 2024-04-24

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