Structure of PDB 7ydb Chain B

Receptor sequence

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

EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLS
SQRLIKEACDESRFDKNLSQALKFVRDFAGDGLVTSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKR
QFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDEN
IRYQIITFLIAGHEITSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVP
SYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEL
MVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKI
PL

3D structure

• PDB: 7ydb Regiodivergent and Enantioselective Hydroxylation of C-H bonds by Synergistic Use of Protein Engineering and Exogenous Dual-Functional Small Molecules.
• Chain: B
• Resolution: 1.472 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 V87 W96 F261 A264 I268 T269 L272 A328 F331 P392 F393 G394 R398 C400 I401 G402 A406	K66 L83 V84 W93 F258 A261 I265 T266 L269 A325 F328 P389 F390 G391 R395 C397 I398 G399 A403
BS02	PYJ	B	L75 V78 V87 I263 L437	L72 V75 V84 I260 L434
BS03	IRV	B	L20 P25 Y51 L188 A328 A330	L17 P22 Y48 L185 A325 A327

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