Structure of PDB 6j86 Chain B

Receptor sequence
>6j86B (length=396) Species: 2017 (Streptoalloteichus hindustanus) [Search protein sequence]
GTPAPVRYPFGEAVRLDLHPTYAELRERRTLLRVRVPHGDDAWLVTRHED
VRTVLTDPRFSRAAAAGRDEARLTPLVIRTSVMGVDPPDHTRLRRLVATA
FSRRGVEHLRPGITALVRRLTDDMVGQGPPVDLVRSFVTPLSGLVICDLL
GVPYADRSRFRHWLEAFFSITALPADEVAVRIEAMYGYIAELVALRRAEP
TEDLLGGLVRARDRDGSCSEEELVDLANVLLLAGYHTTASQLASSLFVLL
TQPEHAELLRSRPELAPRAVEELLRYVPLIAHVTFARYATEDVWLGGTLV
RAGEAVLPAVPSANRDAEVFDEPDRLDLTRRHNPHLAFGHGLHHCLGASL
VRVQMEVALTMLLGRFPDLALAAPPDEVPWTRGMQARSPLRLPVTW
3D structure
PDB6j86 Molecular basis for the P450-catalyzed C-N bond formation in indolactam biosynthesis.
ChainB
Resolution2.6 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) S169 H236 T237 C345 L346 G347
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 B V84 M85 H92 R96 F103 L232 A235 T240 Q243 T286 R289 A339 F340 H345 C347 L348 G349 V353 V82 M83 H90 R94 F101 L230 A233 T238 Q241 T284 R287 A337 F338 H343 C345 L346 G347 V351
BS02 B9L B M85 F170 V231 T239 T286 F287 Q387 M83 F168 V229 T237 T284 F285 Q385
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:6j86, PDBe:6j86, PDBj:6j86
PDBsum6j86
PubMed31636430
UniProtA0A1M4Y7D5

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