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2WIO

Structure of the histidine tagged, open cytochrome P450 Eryk from S. erythraea

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
A0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A0017000biological_processantibiotic biosynthetic process
A0020037molecular_functionheme binding
A0033068biological_processmacrolide biosynthetic process
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 1412
ChainResidue
AILE87
ATHR246
ALEU249
APHE288
AARG293
ASER345
APHE346
AGLY347
AHIS351
ACYS353
AGLY355
AHIS88
ALEU358
AALA359
AHOH2078
AHOH2306
AHOH2307
AHOH2308
AHIS95
AARG99
APHE106
ALEU238
AALA241
AGLY242
ATHR245

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGVHFCLG
ChainResidueDetails
APHE346-GLY355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AHIS88
AHIS95
AARG99
AGLN292
AARG293
AHIS351

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS353

218853

PDB entries from 2024-04-24

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