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3A4G

Structure of cytochrome P450 vdh from Pseudonocardia autotrophica (trigonal crystal form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
A0047103molecular_function3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity
A0047748molecular_functioncholestanetetraol 26-dehydrogenase activity
A0047749molecular_functioncholestanetriol 26-monooxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 412
ChainResidue
APHE58
ATHR241
APRO287
AARG289
ALEU312
APHE339
APHE340
AGLY341
AILE344
AHIS345
ACYS347
ALYS65
AGLY349
AALA353
APG0420
AHOH508
AHOH763
AMET87
AILE88
AHIS95
AARG99
AALA236
AGLY237
ATHR240

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG0 A 420
ChainResidue
AILE88
ALEU232
AHEM412
AHOH622
AHOH763

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P0A512
ChainResidueDetails
ACYS347

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PDB entries from 2024-06-12

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