Structure of PDB 5l90 Chain A

Receptor sequence
>5l90A (length=385) Species: 592022 (Priestia megaterium DSM 319) [Search protein sequence]
ERFNPFSWYEEMRNTAPVQWDEERQVWDVFHYDGVKEVLEQKNIFSSDRR
PPQNQRQTALGTSLINIDPPKHAEMRALVNKAFTPKAMKAWEPKIARITN
ELLQEVEHLEDIDIVEHLSYPLPVMVIADILGVPIEDQRQFKDWSDIIVA
GPSNNERETLEKLQQEKMKANDELETYFYRIIEEKRTRPGDDIISVLLQA
KEEGKQLTDEEIVGFSILLLIAGNETTTNLISNTIYCLMEDKASFERLKR
EKELLPSGIEEVLRYRSPVQALHRIVKEDVTLAGKKLKAGEHVVPWMGSA
HRDAEYFEDPEVFKIDRKPNVHMAFGRGIHFCLGAPLARIEAKIMLAELI
DRYPQMDWSPSFELKPIESTFVYGLKELLIRKNVH
3D structure
PDB5l90 Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium.
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A170 A242 E245 T246 T247 F345 C352 L353 G354 E361 V392
Catalytic site (residue number reindexed from 1) A150 A222 E225 T226 T227 F325 C332 L333 G334 E341 V372
Enzyme Commision number 1.14.14.-
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 L84 I85 H92 R96 A242 G243 T246 L250 L292 R294 A344 F345 H350 C352 G354 A358 L64 I65 H72 R76 A222 G223 T226 L230 L272 R274 A324 F325 H330 C332 G334 A338
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
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:5l90, PDBe:5l90, PDBj:5l90
PDBsum5l90
PubMed27686671
UniProtD5DKI8

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