Structure of PDB 8u2m Chain B

Receptor sequence
>8u2mB (length=382) Species: 2094022 (Micromonospora sp. MW-13) [Search protein sequence]
PIYDPLAPSVIADPYPFYRKLRETNTVHWHEFLDSWVVTGYAECRQVLGD
TTNFGSDFRRIDVEIPDTQLSVQSLDPPEHGAIRHLLVSALHEQPLSTVR
QQFAAIAAQHLAELSGQPGTVDLVSRFARPVALRTITAFLGVPPPDGAGF
EQWSNAIVRSMDAGIEPARAEPGNQARAELSRLVTHWLAEADERGFVGAA
RRAARAQDVPAAVLANSLRAVLHAGYESVSRLLGGVLARLVRHPELLAGP
ATRDADEALVDELIRLDGPVQADARVCVRDQPVGAQLVRRGDVLVLFIAA
ANRDPAVFPDPDAVRLTRRRGLHLAFGRGAHACLGAGLATLQLREVLGAL
RAGGLRLAPAGPAAYEPTATLRGLAELPVSVR
3D structure
PDB8u2m Structural Insights into a Side Chain Cross-Linking Biarylitide P450 from RiPP Biosynthesis
ChainB
Resolution1.79 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.-.-
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 MRY B E104 A210 R213 A214 E93 A199 R202 A203
BS02 HEM B V83 H91 R95 G236 S239 V240 D284 R286 A336 F337 H342 C344 A350 V72 H80 R84 G225 S228 V229 D273 R275 A325 F326 H331 C333 A339
BS03 TFA B R250 H254 L257 V325 R239 H243 L246 V314
BS04 TFA B L258 L361 R367 L368 L247 L350 R356 L357
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:8u2m, PDBe:8u2m, PDBj:8u2m
PDBsum8u2m
PubMed
UniProtA0A3E2YLT4

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