Structure of PDB 5esi Chain A

Receptor sequence
>5esiA (length=530) Species: 307796 (Saccharomyces cerevisiae YJM789) [Search protein sequence]
SIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDR
PPLVFYWIPWVGSAVVYWMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLG
PKGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVK
GALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTI
FTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRD
HAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIA
NLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKEL
TYDLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYH
VLVSPGYTHLRDEYFPNAHQFNIHRWNNDSASSYSVGEEVDYGFGAISKG
VSSPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPD
FTSMVTLPTGPAKIIWEKRNPEQKIGGRHH
3D structure
PDB5esi Impact of Homologous Resistance Mutations from Pathogenic Yeast on Saccharomyces cerevisiae Lanosterol 14 alpha-Demethylase.
ChainA
Resolution2.1 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) T313 F458 C465
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 L147 K151 V311 G314 G315 T318 P379 L383 R385 P462 F463 H468 C470 G472 Y121 Y135 L142 K146 V306 G309 G310 T313 P374 L378 R380 P457 F458 H463 C465 G467
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:5esi, PDBe:5esi, PDBj:5esi
PDBsum5esi
PubMed29263059
UniProtA6ZSR0

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