Structure of PDB 5l94 Chain B

Receptor sequence
>5l94B (length=360) Species: 592022 (Priestia megaterium DSM 319) [Search protein sequence]
FNPFSWYEEMRNTAPVQWDEERQVWDVFHYDGVKEVLEQKNIFSSDGTSL
INIDPPKHAEMRALVNKAFTPKAMKAWEPKIARITNELLQEVEHLEDIDI
VEHLSYPLPVMVIADILGVPIEDQRQFKDWSDIIVLEKLQQEKMKANDEL
ETYFYRIIEEKRTRPGDDIISVLLQAKEEGKQLTDEEIVGFSILLLIAGN
ETTTNLISNTIYCLMEDKASFERLKREKELLPSGIEEVLRYRSPVQALHR
IVKEDVTLAGKKLKAGEHVVPWMGSAHRDAEYFEDPEVFKIDRKPNVHMA
FGRGIHFCLGAPLARIEAKIMLAELIDRYPQMDWSPSFELKPIESTFVYG
LKELLIRKNV
3D structure
PDB5l94 Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium.
ChainB
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A242 E245 T246 T247 F345 C352 L353 G354 E361 V392
Catalytic site (residue number reindexed from 1) A198 E201 T202 T203 F301 C308 L309 G310 E317 V348
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 B L84 I85 H92 R96 A242 G243 T246 T247 L250 L292 R294 A344 F345 G346 H350 C352 G354 A358 L50 I51 H58 R62 A198 G199 T202 T203 L206 L248 R250 A300 F301 G302 H306 C308 G310 A314
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:5l94, PDBe:5l94, PDBj:5l94
PDBsum5l94
PubMed27686671
UniProtD5DKI8

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