Structure of PDB 5zlh Chain D

Receptor sequence
>5zlhD (length=451) Species: 1404 (Priestia megaterium) [Search protein sequence]
MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSS
QRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILL
PSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIG
LCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQ
FQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENI
RYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPS
YKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELM
VLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQ
FALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIP
L
3D structure
PDB5zlh Reconstitution of full-length P450BM3 with an artificial metal complex by utilising the transpeptidase Sortase A.
ChainD
Resolution3.4 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) T264 F389 C396
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 D K69 L86 F87 F107 A264 G265 T268 L272 T327 A328 F331 P392 R398 C400 I401 G402 F405 A406 K65 L82 F83 F103 A260 G261 T264 L268 T323 A324 F327 P388 R394 C396 I397 G398 F401 A402
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:5zlh, PDBe:5zlh, PDBj:5zlh
PDBsum5zlh
PubMed29845154
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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