Structure of PDB 4dub Chain A

Receptor sequence
>4dubA (length=456) Species: 1404 (Priestia megaterium) [Search protein sequence]
IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRY
LSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHN
ILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDEN
KRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDD
ENIRYQIITFLAAGHEATSGLLSFALYFLVKNPHVLQKAAEEAARVLVDP
VPSYKQVKQLKYVGMVLNEALRLWPTGPAFSLYAKEDTVLGGEYPLEKGD
ELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACI
GQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLVLKPEGFVVKAKSK
KIPLGG
3D structure
PDB4dub Structure-guided directed evolution of highly selective p450-based magnetic resonance imaging sensors for dopamine and serotonin.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A268 F393 C400
Catalytic site (residue number reindexed from 1) A267 F392 C399
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 A268 T269 F331 P392 F393 G394 R398 C400 I401 G402 A406 K68 L85 F86 W95 G264 A267 T268 F330 P391 F392 G393 R397 C399 I400 G401 A405
BS02 LDP A A264 G328 A330 L437 A263 G327 A329 L436 MOAD: Kd=1.3uM
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:4dub, PDBe:4dub, PDBj:4dub
PDBsum4dub
PubMed22659321
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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