Structure of PDB 5l92 Chain B

Receptor sequence
>5l92B (length=370) Species: 592022 (Priestia megaterium DSM 319) [Search protein sequence]
KEERFNPFSWYEEMRNTAPVQWDEERQVWDVFHYDGVKEVLEQKNIFSSD
GTSLINIDPPKHAEMRALVNKAFTPKAMKAWEPKIARITNELLQEVEHLE
DIDIVEHLSYPLPVMVIADILGVPIEDQRQFKDWSDIIVNNERETLEKLQ
QEKMKANDELETYFYRIIEEKRTRPGDDIISVLLQAKEEGKQLTDEEIVG
FSILLLIAGNETTTNLISNTIYCLMEDKASFERLKREKELLPSGIEEVLR
YRSPVQALHRIVKEDVTLAGKKLKAGEHVVPWMGSAHRDAEYFEDPEVFK
IDRKPNVHMAFGRGIHFCLGAPLARIEAKIMLAELIDRYPQMDWSPSFEL
KPIESTFVYGLKELLIRKNV
3D structure
PDB5l92 Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A242 E245 T246 T247 F345 C352 L353 G354 E361 V392
Catalytic site (residue number reindexed from 1) A208 E211 T212 T213 F311 C318 L319 G320 E327 V358
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 H92 R96 A242 G243 T246 T247 L250 L292 R294 A344 F345 H350 C352 G354 A358 L54 H62 R66 A208 G209 T212 T213 L216 L258 R260 A310 F311 H316 C318 G320 A324
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:5l92, PDBe:5l92, PDBj:5l92
PDBsum5l92
PubMed27686671
UniProtD5DKI8

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