Structure of PDB 8jc4 Chain B

Receptor sequence

>8jc4B (length=448) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581)

KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRAPAYDENKRQFQ
EDIKVMNDLVDKIIADRKSGEQSDDLLTHMLNGKDPETGEPLDDENIRYQ
IITFLIAGHEVTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQ
VKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLI
PQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFAL
HEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL

3D structure

• PDB: 8jc4 C(sp3)-H hydroxylation of Broad-Spectrum Alkanes Catalyzed by an Artificial P450 Peroxygenase Driven by omega-Pyridyl Fatty Acyl Amino Acids.
• Chain: B
• Resolution: 2.64 Å

Enzymatic activity

• 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 A87 W96 F107 F261 A264 T269 T327 A328 F331 P392 F393 G394 R398 C400 A406	K67 L84 A85 W94 F105 F254 A257 T262 T320 A321 F324 P385 F386 G387 R391 C393 A399
BS02	PHE	B	L20 P25 Y51 L188	L18 P23 Y49 L186
BS03	UCH	B	Y51 P329 A330 L437	Y49 P322 A323 L430
BS04	PHE	B	L20 R47 Y51 S72 Q73 A74	L18 R45 Y49 S70 Q71 A72

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

External links

• PDB: RCSB:8jc4, PDBe:8jc4, PDBj:8jc4
• PDBsum: 8jc4
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)