Structure of PDB 5m0n Chain A

Receptor sequence
>5m0nA (length=423) Species: 946435 (Jeotgalicoccus sp. ATCC 8456) [Search protein sequence]
HMATLKRDKGLDNTLKVLKQGYLYTTNQRNRLNTSVFQTKALGGKPFVVV
TGKEGAEMFYNNDVVQREGMLPKRIVNTLFGKGAIHTVDGKKHVDRKALF
MSLMTEGNLNYVRELTRTLWHANTQRMESMDEVNIYRESIVLLTKVGTRW
AGVQAPPEDIERIATDMDIMIDSFRALGGAFKGYKASKEARRRVEDWLEE
QIIETRKGNIHPPEGTALYEFAHWEDYLGNPMDSRTCAIDLMNTFRPLIA
INRFVSFGLHAMNENPITREKIKSEPDYAYKFAQEVRRYYPFVPFLPGKA
KVDIDFQGVTIPAGVGLALDVYGTTHDESLWDDPNEFRPERFETWDGSPF
DLIPQGGGDYWTNHRCAGEWITVIIMEETMKYFAEKITYDVPEQDLEVDL
NSIPGYVKSGFVIKNVREVVDRT
3D structure
PDB5m0n Catalytic Determinants of Alkene Production by the Cytochrome P450 Peroxygenase OleTJE.
ChainA
Resolution1.44 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 A Y59 R66 H85 H92 K96 F99 N242 T243 P246 L247 A249 I250 F291 L295 Q354 H363 C365 G367 T371 Y60 R67 H86 H93 K97 F100 N243 T244 P247 L248 A250 I251 F292 L296 Q355 H364 C366 G368 T372
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:5m0n, PDBe:5m0n, PDBj:5m0n
PDBsum5m0n
PubMed28053093
UniProtE9NSU2

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