Structure of PDB 5zis Chain A

Receptor sequence
>5zisA (length=452) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581) [Search protein sequence]
EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLS
SQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKR
QFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDEN
IRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVP
SYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEL
MVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKI
PL
3D structure
PDB5zis Reconstitution of full-length P450BM3 with an artificial metal complex by utilising the transpeptidase Sortase A.
ChainA
Resolution3.1 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) T265 F390 C397
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 MNH A K69 L86 F87 A264 G265 T268 T269 L272 A328 F331 F393 R398 C400 F405 A406 K66 L83 F84 A261 G262 T265 T266 L269 A325 F328 F390 R395 C397 F402 A403
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:5zis, PDBe:5zis, PDBj:5zis
PDBsum5zis
PubMed29845154
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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