Structure of PDB 5m0o Chain C

Receptor sequence
>5m0oC (length=421) Species: 946435 (Jeotgalicoccus sp. ATCC 8456) [Search protein sequence]
HHMATLKRDKGLDNTLKVLKQGYLYTTNQRNRLNTSVFQTKALGGKPFVV
VTGKEGAEMFYNNDVVQREGMLPKRIVNTLFGKGAIQTVDGKKHVDRKAL
FMSLMTEGNLNYVRELTRTLWHANTQRMESMDEVNIYRESIVLLTKVGTR
WAGVQAPPEDIERIATDMDIMIDSFRALGGAFKGYKASKEARRRVEDWLE
EQIIETRIHPPEGTALYEFAHWEDYLGNPMDSRTCAIDLMNTFRPLIAIN
RFVSFGLHAMNENPITREKIKSEPDYAYKFAQEVRRYYPFVPFLPGKAKV
DIDFQGVTIPAGVGLALDVYGTTHDESLWDDPNEFRPERFETWDGSPFDL
IPQGGGDYWTNHRCAGEWITVIIMEETMKYFAEKITYDVPEQDLEVDLNS
IPGYVKSGFVIKNVREVVDRT
3D structure
PDB5m0o Catalytic Determinants of Alkene Production by the Cytochrome P450 Peroxygenase OleTJE.
ChainC
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 C Y59 R66 H92 K96 F99 T243 P246 L247 I250 L295 Q354 H363 C365 G367 Y61 R68 H94 K98 F101 T242 P245 L246 I249 L294 Q353 H362 C364 G366
BS02 EPA C F173 R245 P246 F291 F175 R244 P245 F290
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0016125 sterol metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5m0o, PDBe:5m0o, PDBj:5m0o
PDBsum5m0o
PubMed28053093
UniProtE9NSU2

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