Structure of PDB 5jtd Chain B

Receptor sequence
>5jtdB (length=458) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLD
DENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVD
PVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKG
DELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFACHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKS
KKIPLGGI
3D structure
PDB5jtd Insights into an efficient light-driven hybrid P450 BM3 enzyme from crystallographic, spectroscopic and biochemical studies.
ChainB
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T268 F393 C400
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.6.2.4: NADPH--hemoprotein reductase.
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 K69 L86 F87 W96 A264 T269 F331 P392 F393 R398 C400 I401 G402 K69 L86 F87 W96 A264 T269 F331 P392 F393 R398 C400 I401 G402
BS02 RU8 B K309 K312 G315 M316 N319 P382 C407 K309 K312 G315 M316 N319 P382 C407
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

View graph for
Molecular Function
External links
PDB RCSB:5jtd, PDBe:5jtd, PDBj:5jtd
PDBsum5jtd
PubMed27639964
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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