Structure of PDB 5eaf Chain A

Receptor sequence
>5eafA (length=528) Species: 307796 (Saccharomyces cerevisiae YJM789) [Search protein sequence]
VGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPP
LVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPK
GHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGA
LTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIFT
ASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHA
QKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIANL
LIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELTY
DLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYAIPAGYHVL
VSPGYTHLRDEYFPNAHQFNIHRWNNDSASSYSVGEEVDYGFGAISKGVS
SPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPDFT
SMVTLPTGPAKIIWEKRNPEQKIGGRHH
3D structure
PDB5eaf Structural and Functional Elucidation of Yeast Lanosterol 14 alpha-Demethylase in Complex with Agrochemical Antifungals.
ChainA
Resolution2.65 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
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 Y126 Y140 K151 G315 T318 P379 L383 R385 P462 F463 H468 C470 G472 Y119 Y133 K144 G308 T311 P372 L376 R378 P455 F456 H461 C463 G465
BS02 FQC A Y126 F134 G310 G314 L380 Y119 F127 G303 G307 L373
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:5eaf, PDBe:5eaf, PDBj:5eaf
PDBsum5eaf
PubMed27907120
UniProtA6ZSR0

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