Structure of PDB 7ydd Chain B

Receptor sequence

>7yddB (length=453) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581)

KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFIRDFAGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENK
RQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDE
NIRYQIITFLIAGHEPTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPV
PSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDE
LMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIG
QQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKK
IPL

3D structure

• PDB: 7ydd Regiodivergent and Enantioselective Hydroxylation of C-H bonds by Synergistic Use of Protein Engineering and Exogenous Dual-Functional Small Molecules.
• Chain: B
• Resolution: 1.663 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	3H0	B	L75 I78 A87 A264	L73 I76 A85 A262
BS02	HEM	B	K69 L86 A87 W96 F107 F261 A264 G265 P268 T269 F331 P392 F393 R398 C400 G402 A406	K67 L84 A85 W94 F105 F259 A262 G263 P266 T267 F329 P390 F391 R396 C398 G400 A404
BS03	IRV	B	L20 F42 R47 Y51 S72 Q73 A74 A328 P329 A330	L18 F40 R45 Y49 S70 Q71 A72 A326 P327 A328

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