Structure of PDB 5ucw Chain A

Receptor sequence
>5ucwA (length=453) Species: 1404 (Priestia megaterium) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFLGDGLATSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVSEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFIISMVRALDEVMNKLQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRKARGEQSDDLLTQMLNGKDPETGEPLD
DGNIRYQIITFLLAGHEGTSGLLSFALYFLVKNPHVLQKVAEEAARVLVD
PVPSYKQVKQLKYVGMVLNEALRLWPTVPAFSLYAKEDTVLGGEYPLEKG
DEVMVLIPQLHRDKTVWGDDVEEFRPERFENAIPQHAFKPFGNGQRASIG
QQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLSLKPKGFVVKAKSKK
IPL
3D structure
PDB5ucw Enantioselective, intermolecular benzylic C-H amination catalysed by an engineered iron-haem enzyme.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G268 F393 S400
Catalytic site (residue number reindexed from 1) G268 F391 S398
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 A87 W96 A264 G265 G268 T269 V328 F331 P392 F393 R398 S400 I401 G402 A406 K69 L86 A87 W96 A264 G265 G268 T269 V328 F331 P390 F391 R396 S398 I399 G400 A404
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:5ucw, PDBe:5ucw, PDBj:5ucw
PDBsum5ucw
PubMed28644476
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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