Structure of PDB 5dyz Chain A

Receptor sequence
>5dyzA (length=445) Species: 1404 (Priestia megaterium) [Search protein sequence]
IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRY
LSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHN
ILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRENKRQFQEDIK
VMNDLVDKIIADRKASEQSDDLLTHMLNGKDPETGEPLDGENIRYQIITF
LIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKHVKQL
KYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLH
RDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEAT
LVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLG
3D structure
PDB5dyz Subtle structural changes in the Asp251Gly/Gln307His P450 BM3 mutant responsible for new activity toward diclofenac, tolbutamide and ibuprofen.
ChainA
Resolution1.967 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T257 F382 C389
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 F107 F261 A264 G265 T268 A328 F331 P392 F393 R398 C400 I401 A406 K68 L85 F86 W95 F106 F250 A253 G254 T257 A317 F320 P381 F382 R387 C389 I390 A395
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

View graph for
Molecular Function
External links
PDB RCSB:5dyz, PDBe:5dyz, PDBj:5dyz
PDBsum5dyz
PubMed26718083
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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