Structure of PDB 4ze2 Chain A

Receptor sequence
>4ze2A (length=529) Species: 307796 (Saccharomyces cerevisiae YJM789) [Search protein sequence]
SIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDR
PPLVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLG
PKGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIHDCPNSRLMEQKKFVK
GALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTI
FTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRD
HAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIA
NLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKEL
TYDLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYH
VLVSPGYTHLRDEYFPNAHQFNIHRWNNDSASSYSVGEEVDYGFGAISKG
VSSPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPD
FTSMVTLPTGPAKIIWEKRNPEQKIGGRH
3D structure
PDB4ze2 Triazole resistance mediated by mutations of a conserved active site tyrosine in fungal lanosterol 14 alpha-demethylase.
ChainA
Resolution2.3 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 L147 K151 G315 T318 P379 L383 R385 P462 F463 H468 C470 G472 Y121 L142 K146 G310 T313 P374 L378 R380 P457 F458 H463 C465 G467
BS02 1YN A A69 Y72 G73 Y126 F134 F236 P238 G310 V311 G314 L380 T507 S508 M509 A64 Y67 G68 Y121 F129 F231 P233 G305 V306 G309 L375 T502 S503 M504 MOAD: Kd=0.13uM
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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Biological Process
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Cellular Component
External links
PDB RCSB:4ze2, PDBe:4ze2, PDBj:4ze2
PDBsum4ze2
PubMed27188873
UniProtA6ZSR0

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