Structure of PDB 3p3o Chain A

Receptor sequence
>3p3oA (length=416) Species: 66431 (Streptomyces thioluteus) [Search protein sequence]
ISEFDSEGSNMSTTAHTEPSWADLPFLDFTDPNFSWDSPEVAEAREKSWI
ARTPLALLVLRYAEADQLARDKRLISGFRGLVDMVGTPEGPVRDFMVDFL
QSLDGADHRRLRGLATHPFTPRRITAVQPFVRSTVEQLIDKLPQGDFDFV
QHFPHPLPALVMCQLLGFPLEDYDTVGRLSIETNLGLALSNDQDILVKVE
QGLGRMFDYLVAAIEKRKVEPGDDLTSDIVRAFHDGVLDDYELRTLVATV
LVAGYETTNHQLALAMYDFAQHPDQWMKIKENPELAPQAVEEVLRWSPTL
PVTATRVAAEDFEVNGVRIPTGTPVFMCAHVAHRDPRVFADADRFDITVK
REAPSIAFGGGPHFCLGTALARLELTEAVAALATRLDPPQIAGEITWRHE
LGVAGPDALPLRFGAA
3D structure
PDB3p3o Structural fine-tuning of a multifunctional cytochrome p450 monooxygenase.
ChainA
Resolution1.54 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) L185 A253 E256 T257 T258 L300 C365 L366 G367 E374 V403
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 F109 M152 A243 G244 T247 T248 Q251 L290 T293 R296 A347 F348 G350 H353 C355 L356 G357 A361 L100 Q101 H108 R112 F119 M162 A253 G254 T257 T258 Q261 L300 T303 R306 A357 F358 G360 H363 C365 L366 G367 A371
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:3p3o, PDBe:3p3o, PDBj:3p3o
PDBsum3p3o
PubMed21280577
UniProtQ70KH6

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