Structure of PDB 3ekf Chain A

Receptor sequence
>3ekfA (length=441) Species: 1404 (Priestia megaterium) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANQFQEKVMN
DLVDKIIADRKASQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIQG
HETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVG
MVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKT
IWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLG
MMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLG
3D structure
PDB3ekf Novel haem co-ordination variants of flavocytochrome P450BM3.
ChainA
Resolution2.1 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) 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 F261 Q264 G265 T268 F331 P392 F393 R398 C400 I401 G402 A406 K69 L86 F87 W96 F246 Q249 G250 T253 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

View graph for
Molecular Function
External links
PDB RCSB:3ekf, PDBe:3ekf, PDBj:3ekf
PDBsum3ekf
PubMed18721129
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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