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5L1T

X-ray Structure of M77S mutant of Cytochrome P450 PntM with pentalenolactone F

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0017000biological_processantibiotic biosynthetic process
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
A0055114biological_processobsolete oxidation-reduction process
A1901780biological_processpentalenolactone biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue 7PF A 401
ChainResidue
AARG74
AHOH629
AHOH678
AHOH688
ATHR236
AARG240
AASN283
ALEU285
APRO287
AILE387
ATHR388
AHEM402

site_idAC2
Number of Residues18
Detailsbinding site for residue HEM A 402
ChainResidue
AMET81
AHIS93
AARG97
APHE232
AGLY233
ATHR236
ATHR237
AARG240
AILE286
AARG288
AALA339
APHE340
AARG345
ACYS347
AGLY349
A7PF401
AHOH576
AHOH629

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

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

221051

PDB entries from 2024-06-12

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