Structure of PDB 6j82 Chain A

Receptor sequence
>6j82A (length=392) Species: 68180 (Streptomyces blastmyceticus) [Search protein sequence]
PLSYPFNEAVALDVDPLYAKLRAEEPVVRVSCPFGEDAWLVTSHADMKTI
LADPRFSRALAAEHDESRLTPLPIHTSILGMDSPDHTRLRRLLAKVFTMR
RVELLRPRIEQEADRLIDALIAEGPPGDLMEGFAVPFAGTVVCDLLGVPF
EDREQFRGWLDAFSATTVMTEEEIEADTERLHGYIAQLMVRRRAEPQDDL
ISAMVKASDEEEKLSEKELVELASVLLIAGHETVSSQLIDSLHVLFTHPE
QLRLLKDRPELMPGTVEELMRFVPLISHVTFARYATEDVELSGTLVRAGE
SVLPAIPSANRDESVFENADRFDLTREHNPHLGFGYGIHRCLGAPLARLE
MQVALDSLLRRLPELRCAVPAESLEWKDGMQVRSLLELPVLW
3D structure
PDB6j82 Molecular basis for the P450-catalyzed C-N bond formation in indolactam biosynthesis.
ChainA
Resolution2.202 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) A171 E238 T239 C347 L348 G349
Catalytic site (residue number reindexed from 1) A165 E232 T233 C341 L342 G343
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 I84 L85 H92 R96 F103 L232 A235 T239 V240 Q243 T286 R289 G339 F340 G341 H345 C347 G349 I78 L79 H86 R90 F97 L226 A229 T233 V234 Q237 T280 R283 G333 F334 G335 H339 C341 G343
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:6j82, PDBe:6j82, PDBj:6j82
PDBsum6j82
PubMed31636430
UniProtA0A077KEB8

[Back to BioLiP]