Structure of PDB 1ee0 Chain A

Receptor sequence
>1ee0A (length=376) Species: 18101 (Gerbera hybrid cultivar) [Search protein sequence]
GLATILAIGTATPPNCVAQADYADYYFRVTKSEHMVDLKEKFKRICEKTA
IKKRYLALTEDYLQENPTMCEFMAPSLNARQDLVVTGVPMLGKEAAVKAI
DEWGLPKSKITHLIFCTTAGVDMPGADYQLVKLLGLSPSVKRYMLYQQGC
AAGGTVLRLAKDLAENNKGSRVLIVCSEITAILFHGPNENHLDSLVAQAL
FGDGAAALIVGSGPHLAVERPIFEIVSTDQTILPDTEKAMKLHLREGGLT
FQLHRDVPLMVAKNIENAAEKALSPLGITDWNSVFWMVHPGGRAILDQVE
RKLNLKEDKLRASRHVLSEYGNLISACVLFIIDEVRKRSMAEGKSTTGEG
LDCGVLFGFGPGMTVETVVLRSVRVT
3D structure
PDB1ee0 Structural control of polyketide formation in plant-specific polyketide synthases.
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C169 F220 H308 N341
Catalytic site (residue number reindexed from 1) C150 F201 H289 N322
Enzyme Commision number 2.3.1.-
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 CAA A K60 R63 I64 K67 A169 D212 V215 M259 L261 L272 R274 G310 G311 R312 A313 K41 R44 I45 K48 A150 D193 V196 M240 L242 L253 R255 G291 G292 R293 A294
Gene Ontology
Molecular Function
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0009058 biosynthetic process
GO:0030639 polyketide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1ee0, PDBe:1ee0, PDBj:1ee0
PDBsum1ee0
PubMed11137815
UniProtP48391|2PS_GERHY 2-pyrone synthase (Gene Name=2PS)

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