Structure of PDB 4du2 Chain A

Receptor sequence
>4du2A (length=443) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQAPKFVRDLAGDGLFTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLRENKRQFQEDIKVM
NDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFL
AAGHEATSGLLSFALYFLVKNPHELQKAAEEAARVLVDPVPSHKQVKQLK
YVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHR
DKTVWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATL
VLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB4du2 Structure-guided directed evolution of highly selective p450-based magnetic resonance imaging sensors for dopamine and serotonin.
ChainA
Resolution1.9 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) A256 F381 C388
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 A328 F331 P392 F393 R398 C400 I401 G402 K67 L84 F85 W94 G253 A256 T257 A316 F319 P380 F381 R386 C388 I389 G390
BS02 LDP A A74 F87 A264 A328 P329 A330 L437 A72 F85 A252 A316 P317 A318 L425 MOAD: Kd=3.3uM
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:4du2, PDBe:4du2, PDBj:4du2
PDBsum4du2
PubMed22659321
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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