Structure of PDB 2x7y Chain B

Receptor sequence
>2x7yB (length=439) Species: 1404 (Priestia megaterium) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLATSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLNKRQFQEDIKVM
NDLVDKIIADRKASDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGH
ETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGM
VLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTI
WGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGM
MLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB2x7y The Role of Active-Site Phe87 in Modulating the Organic Co-Solvent Tolerance of Cytochrome P450 Bm3 Monooxygenase.
ChainB
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) T252 F377 C384
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 B K69 L86 A87 W96 F107 F261 A264 G265 T268 A328 F331 P392 F393 R398 C400 I401 G402 A406 K69 L86 A87 W96 F107 F245 A248 G249 T252 A312 F315 P376 F377 R382 C384 I385 G386 A390
BS02 ZN B D231 H236 D215 H220
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:2x7y, PDBe:2x7y, PDBj:2x7y
PDBsum2x7y
PubMed22949185
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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