Structure of PDB 4zdy Chain A

Receptor sequence
>4zdyA (length=527) Species: 307796 (Saccharomyces cerevisiae YJM789) [Search protein sequence]
VGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPP
LVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPK
GHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIFDCPNSRLMEQKKFVKGA
LTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIFT
ASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHA
QKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIANL
LIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELTY
DLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHVL
VSPGYTHLRDEYFPNAHQFNIHRWNNDSASSYSVGEEVDYGFGAISKGVS
SPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPDFT
SMVTLPTGPAKIIWEKRNPEQKIGGRH
3D structure
PDB4zdy Triazole resistance mediated by mutations of a conserved active site tyrosine in fungal lanosterol 14 alpha-demethylase.
ChainA
Resolution2.02 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4zdy, PDBe:4zdy, PDBj:4zdy
PDBsum4zdy
PubMed27188873
UniProtA6ZSR0

[Back to BioLiP]