Structure of PDB 3psx Chain A

Receptor sequence
>3psxA (length=412) Species: 1404 (Priestia megaterium) [Search protein sequence]
EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLS
SQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPVMNDLVDKIIADRKASQSDDLLTHMLHGKDP
ETGEPLDDENIRYQIVTFLIAGHETTSGLLSFTLYFLVKNPHVLQKAAEE
AARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGG
EYPLEKGDEIMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPF
GNGQRACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEG
FVVKAKSKKIPL
3D structure
PDB3psx Structure, electronic properties and catalytic behaviour of an activity-enhancing CYP102A1 (P450(BM3)) variant
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) T268 F393 C400
Catalytic site (residue number reindexed from 1) T225 F350 C357
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 A264 G265 T268 T269 F331 P392 F393 R398 C400 I401 G402 F405 A406 K66 L83 F84 W93 F218 A221 G222 T225 T226 F288 P349 F350 R355 C357 I358 G359 F362 A363
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:3psx, PDBe:3psx, PDBj:3psx
PDBsum3psx
PubMed21603690
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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