Structure of PDB 5iki Chain A

Receptor sequence
>5ikiA (length=383) Species: 1404 (Priestia megaterium) [Search protein sequence]
VIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVK
RVLSDYKHFSSVRKSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWE
PRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFK
KWVDTLFLPKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGE
MFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDL
VPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDE
EMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKF
KHIEAVPSFQLEENLTDSATGQTLTSLPLKASR
3D structure
PDB5iki Crystal Structure of CYP106A2 in Substrate-Free and Substrate-Bound Form.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L174 A243 E246 T247 T248 C355 L356 G357 E364 G397
Catalytic site (residue number reindexed from 1) L158 A217 E220 T221 T222 C329 L330 G331 E338 G371
Enzyme Commision number 1.14.15.8: steroid 15beta-monooxygenase.
1.14.99.-
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 I88 T89 H96 R100 F107 A243 G244 T247 F289 L294 R296 T347 F348 H353 C355 G357 A361 I72 T73 H80 R84 F91 A217 G218 T221 F263 L268 R270 T321 F322 H327 C329 G331 A335
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
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:5iki, PDBe:5iki, PDBj:5iki
PDBsum5iki
PubMed26864272
UniProtQ06069|CPXM_PRIMG Cytochrome P450(MEG) (Gene Name=cyp106A2)

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