Structure of PDB 6j85 Chain A

Receptor sequence
>6j85A (length=395) Species: 2017 (Streptoalloteichus hindustanus) [Search protein sequence]
TPAPVRYPFGEAVRLDLHPTYAELRERRTLLRVRVPHGDDAWLVTRHEDV
RTVLTDPRFSRAAAAGRDEARLTPLVIRTSVMGVDPPDHTRLRRLVATAF
SRRGVEHLRPGITALVRRLTDDMVGQGPPVDLVRSFVTPLSGLVICDLLG
VPYADRSRFRHWLEAFFSITALPADEVAVRIEAMYGYIAELVALRRAEPT
EDLLGGLVRARDRDGSCSEEELVDLANVLLLAGYHTTASQLASSLFVLLT
QPEHAELLRSRPELAPRAVEELLRYVPLIAHVTFARYATEDVWLGGTLVR
AGEAVLPAVPSANRDAEVFDEPDRLDLTRRHNPHLAFGHGLHHCLGASLV
RVQMEVALTMLLGRFPDLALAAPPDEVPWTRGMQARSPLRLPVTW
3D structure
PDB6j85 Molecular basis for the P450-catalyzed C-N bond formation in indolactam biosynthesis.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S171 H238 T239 C347 L348 G349
Catalytic site (residue number reindexed from 1) S168 H235 T236 C344 L345 G346
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 V84 M85 H92 R96 F103 A235 T240 Q243 T286 R289 A339 F340 G341 H345 C347 L348 G349 V353 V81 M82 H89 R93 F100 A232 T237 Q240 T283 R286 A336 F337 G338 H342 C344 L345 G346 V350
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:6j85, PDBe:6j85, PDBj:6j85
PDBsum6j85
PubMed31636430
UniProtA0A1M4Y7D5

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