Structure of PDB 5esf Chain A

Receptor sequence
>5esfA (length=524) Species: 307796 (Saccharomyces cerevisiae YJM789) [Search protein sequence]
IVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRP
PLVFYWIPWVGSAVVYEMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGP
KGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKG
ALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIF
TASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDH
AQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIAN
LLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELT
YDLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHV
LVSPGYTHLRDEYFPNAHQFNIHRWNNDSASGEEVDYGFGAISKGVSSPY
LPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPDFTSMV
TLPTGPAKIIWEKRNPEQKIGGRH
3D structure
PDB5esf Impact of Homologous Resistance Mutations from Pathogenic Yeast on Saccharomyces cerevisiae Lanosterol 14 alpha-Demethylase.
ChainA
Resolution2.25 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) T312 F453 C460
Enzyme Commision number 1.14.13.70: Transferred entry: 1.14.14.154.
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 Y140 L147 K151 V311 G315 T318 P379 L383 R385 P462 F463 H468 C470 I471 G472 Y134 L141 K145 V305 G309 T312 P373 L377 R379 P452 F453 H458 C460 I461 G462
BS02 TPF A Y126 F134 G310 G314 T318 L380 Y120 F128 G304 G308 T312 L374
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:5esf, PDBe:5esf, PDBj:5esf
PDBsum5esf
PubMed29263059
UniProtA6ZSR0

[Back to BioLiP]