Structure of PDB 5l94 Chain A

Receptor sequence
>5l94A (length=385) Species: 592022 (Priestia megaterium DSM 319) [Search protein sequence]
QTKEERFNPFSWYEEMRNTAPVQWDEERQVWDVFHYDGVKEVLEQKNIFS
SDRRPQRQTALGTSLINIDPPKHAEMRALVNKAFTPKAMKAWEPKIARIT
NELLQEVEHLEDIDIVEHLSYPLPVMVIADILGVPIEDQRQFKDWSDIIV
AGPSNNERETLEKLQQEKMKANDELETYFYRIIEEKRTRPGDDIISVLLQ
AKEEGKQLTDEEIVGFSILLLIAGNETTTNLISNTIYCLMEDKASFERLK
REKELLPSGIEEVLRYRSPVQALHRIVKEDVTLAGKKLKAGEHVVPWMGS
AHRDAEYFEDPEVFKIDRKPNVHMAFGRGIHFCLGAPLARIEAKIMLAEL
IDRYPQMDWSPSFELKPIESTFVYGLKELLIRKNV
3D structure
PDB5l94 Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium.
ChainA
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) A170 A242 E245 T246 T247 F345 C352 L353 G354 E361 V392
Catalytic site (residue number reindexed from 1) A151 A223 E226 T227 T228 F326 C333 L334 G335 E342 V373
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 T246 L292 R294 A344 F345 H350 C352 L353 G354 A358 L65 I66 H73 R77 A223 T227 L273 R275 A325 F326 H331 C333 L334 G335 A339
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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