Structure of PDB 3p3l Chain A

Receptor sequence
>3p3lA (length=403) Species: 66431 (Streptomyces thioluteus) [Search protein sequence]
TAHTEPSWADLPFLDFTDPNFSWDSPEVAEAREKSWIARTPLALLVLRYA
EADQLARDKRLISGFRGLVDMVGTPEGPVRDFMVDFLQSLDGADHRRLRG
LATHPFTPRRITAVQPFVRSTVEQLIDKLPQGDFDFVQHFAHPLPALVMC
QLLGFPLEDYDTVGRLSIETNLGLALSNDQDILVKVEQGLGRMFDYLVAA
IEKRKVEPGDDLTSDIVRAFHDGVLDDYELRTLVATVLVAGYETTNHQLA
LAMYDFAQHPDQWMKIKENPELAPQAVEEVLRWSPTLPVTATRVAAEDFE
VNGVRIPTGTPVFMCAHVAHRDPRVFADADRFDITVKREAPSIAFGGGPH
FCLGTALARLELTEAVAALATRLDPPQIAGEITWRHELGVAGPDALPLRF
GAA
3D structure
PDB3p3l Structural fine-tuning of a multifunctional cytochrome p450 monooxygenase.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L175 A243 E246 T247 T248 L290 C355 L356 G357 E364 V393
Catalytic site (residue number reindexed from 1) L172 A240 E243 T244 T245 L287 C352 L353 G354 E361 V390
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A L90 Q91 H98 R102 A243 G244 T247 T248 L290 T293 R296 A347 F348 G350 H353 C355 G357 A361 L87 Q88 H95 R99 A240 G241 T244 T245 L287 T290 R293 A344 F345 G347 H350 C352 G354 A358
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0036199 cholest-4-en-3-one 26-monooxygenase activity
GO:0046872 metal ion binding
Biological Process
GO:0006707 cholesterol catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3p3l, PDBe:3p3l, PDBj:3p3l
PDBsum3p3l
PubMed21280577
UniProtQ70KH6

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