Structure of PDB 8u2m Chain A

Receptor sequence

>8u2mA (length=380) Species: 2094022 (Micromonospora sp. MW-13) [Search protein sequence]

YDPLAPSVIADPYPFYRKLRETNTVHWHEFLDSWVVTGYAECRQVLGDTT
NFGSDFRRIDVEIPDTQLSVQSLDPPEHGAIRHLLVSALHEQPLSTVRQQ
FAAIAAQHLAELSGQPGTVDLVSRFARPVALRTITAFLGVPPPDGAGFEQ
WSNAIVRSMDAGIEPARAEPGNQARAELSRLVTHWLAEADERGFVGAARR
AARAQDVPAAVLANSLRAVLHAGYESVSRLLGGVLARLVRHPELLAGPAT
RDADEALVDELIRLDGPVQADARVCVRDQPVGAQLVRRGDVLVLFIAAAN
RDPAVFPDPDAVRLTRRRGLHLAFGRGAHACLGAGLATLQLREVLGALRA
GGLRLAPAGPAAYEPTATLRGLAELPVSVR

3D structure

PDB

8u2m Structural Insights into a Side Chain Cross-Linking Biarylitide P450 from RiPP Biosynthesis

Chain

Resolution

1.79 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)
BS01	peptide	A	Q84 M172 R188 R230 H234 A235 V281 A283 A285 T381 L382	Q71 M159 R175 R217 H221 A222 V268 A270 A272 T368 L369
BS02	HEM	A	V83 Q84 H91 R95 G236 S239 P280 D284 R286 A336 F337 H342 C344	V70 Q71 H78 R82 G223 S226 P267 D271 R273 A323 F324 H329 C331
BS03	MRY	A	P106 L107 S108	P93 L94 S95

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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:8u2m, PDBe:8u2m, PDBj:8u2m
PDBsum	8u2m
PubMed
UniProt	A0A3E2YLT4

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