Structure of PDB 7yjf Chain B

Receptor sequence

>7yjfB (length=452) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581)

EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLS
SQRLIKEACDESRFDKNLSQALKFIRDFAGDGLATSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKR
QFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDEN
IRYQIITFLIAGHEPTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVP
SYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEL
MVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKI
PL

3D structure

• PDB: 7yjf Regiodivergent and Enantioselective Hydroxylation of C-H bonds by Synergistic Use of Protein Engineering and Exogenous Dual-Functional Small Molecules.
• Chain: B
• Resolution: 1.515 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 G265 P268 T269 A328 F331 P392 F393 G394 R398 C400 I401 G402 A406	K66 L83 A84 W93 F104 F258 A261 G262 P265 T266 A325 F328 P389 F390 G391 R395 C397 I398 G399 A403
BS02	HOA	B	A264 P268	A261 P265
BS03	IRV	B	L20 P25 Y51 L188 A328 A330 L437	L17 P22 Y48 L185 A325 A327 L434

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:7yjf, PDBe:7yjf, PDBj:7yjf
• PDBsum: 7yjf
• PubMed: 36417593
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)