Structure of PDB 5l92 Chain A

Receptor sequence
>5l92A (length=386) Species: 592022 (Priestia megaterium DSM 319) [Search protein sequence]
IQTKEERFNPFSWYEEMRNTAPVQWDEERQVWDVFHYDGVKEVLEQKNIF
SSDRRPQRQTALGTSLINIDPPKHAEMRALVNKAFTPKAMKAWEPKIARI
TNELLQEVEHLEDIDIVEHLSYPLPVMVIADILGVPIEDQRQFKDWSDII
VAGPSNNERETLEKLQQEKMKANDELETYFYRIIEEKRTRPGDDIISVLL
QAKEEGKQLTDEEIVGFSILLLIAGNETTTNLISNTIYCLMEDKASFERL
KREKELLPSGIEEVLRYRSPVQALHRIVKEDVTLAGKKLKAGEHVVPWMG
SAHRDAEYFEDPEVFKIDRKPNVHMAFGRGIHFCLGAPLARIEAKIMLAE
LIDRYPQMDWSPSFELKPIESTFVYGLKELLIRKNV
3D structure
PDB5l92 Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium.
ChainA
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) A170 A242 E245 T246 T247 F345 C352 L353 G354 E361 V392
Catalytic site (residue number reindexed from 1) A152 A224 E227 T228 T229 F327 C334 L335 G336 E343 V374
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 L239 A242 T246 L250 L292 R294 A344 F345 H350 C352 L353 G354 A358 L66 I67 H74 R78 L221 A224 T228 L232 L274 R276 A326 F327 H332 C334 L335 G336 A340
BS02 C0R A I168 I241 A242 F391 I150 I223 A224 F373 MOAD: Kd=91uM
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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