Structure of PDB 6j88 Chain B

Receptor sequence
>6j88B (length=395) Species: 2017 (Streptoalloteichus hindustanus) [Search protein sequence]
TPAPVRYPFGEAVRLDLHPTYAELRERRTLLRVRVPHGDDAWLVTRHEDV
RTVLTDPRFSRAAAAGRDEARLTPLVIRTSVMGVDPPDHTRLRRLVATAF
SRRGVEHLRPGITALVRRLTDDMVGQGPPVDLVRSFVTPLSGLVICDLLG
VPYADRSRFRHWLEAFFSITALPADEVAVRIEAMYGYIAELVALRRAEPT
EDLLGGLVRARDRDGSCSEEELVDLANVLLLAGYHTTASQLASSLFVLLT
QPEHAELLRSRPELAPRAVEELLRYVPLIAHVTFARYATEDVWLGGTLVR
AGEAVLPAVPSANRDAEVFDEPDRLDLTRRHNPHLAFGHGLHHCLGASLV
RVQMEVALTMLLGRFPDLALAAPPDEVPWTRGMQARSPLRLPVTW
3D structure
PDB6j88 Molecular basis for the P450-catalyzed C-N bond formation in indolactam biosynthesis.
ChainB
Resolution2.35 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 B L57 V84 M85 R96 F103 L232 A235 G236 T239 T240 Q243 T286 R289 A339 F340 H345 C347 L348 V353 L54 V81 M82 R93 F100 L229 A232 G233 T236 T237 Q240 T283 R286 A336 F337 H342 C344 L345 V350
BS02 B9O B I80 T82 M85 F170 V231 T239 I77 T79 M82 F167 V228 T236
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:6j88, PDBe:6j88, PDBj:6j88
PDBsum6j88
PubMed31636430
UniProtA0A1M4Y7D5

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