Structure of PDB 5esl Chain A

Receptor sequence
>5eslA (length=527) Species: 307796 (Saccharomyces cerevisiae YJM789) [Search protein sequence]
VGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPP
LVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPK
GHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGA
LTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIFT
ASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHA
QKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIANL
LIGVLMGGQHTSAAISAWILLHLAERPDVQQELYEEQMRVLDGGKKELTY
DLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHVL
VSPGYTHLRDEYFPNAHQFNIHRWNNDSASSYSVGEEVDYGFGAISKGVS
SPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPDFT
SMVTLPTGPAKIIWEKRNPEQKIGGRH
3D structure
PDB5esl Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer.
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T318 F463 C470
Catalytic site (residue number reindexed from 1) T311 F456 C463
Enzyme Commision number ?
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008168 methyltransferase activity
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:0006696 ergosterol biosynthetic process
GO:0016126 sterol biosynthetic process
GO:0032259 methylation
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5esl, PDBe:5esl, PDBj:5esl
PDBsum5esl
PubMed
UniProtA6ZSR0

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