Structure of PDB 5dyp Chain A

Receptor sequence

>5dypA (length=440) Species: 1404 (Priestia megaterium)

IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRY
LSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHN
ILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLNKRQFQEDIKVMN
DLVDKIIADRKASQSDDLLTHMLNGKDPETGEPLDGENIRYQIITFLIAG
HETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKHVKQLKYVG
MVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKT
IWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLG
MMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL

3D structure

• PDB: 5dyp Subtle structural changes in the Asp251Gly/Gln307His P450 BM3 mutant responsible for new activity toward diclofenac, tolbutamide and ibuprofen.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T268 F393 C400
• Catalytic site (residue number reindexed from 1): T253 F378 C385
• 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	A	K69 L86 F87 W96 G265 T268 A328 F331 P392 F393 R398 C400 I401 G402 A406	K68 L85 F86 W95 G250 T253 A313 F316 P377 F378 R383 C385 I386 G387 A391

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:5dyp, PDBe:5dyp, PDBj:5dyp
• PDBsum: 5dyp
• PubMed: 26718083
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)