Structure of PDB 1iay Chain A

Receptor sequence
>1iayA (length=419) Species: 4081 (Solanum lycopersicum) [Search protein sequence]
ILSKLATNESPYFDGWKAYDSDPFHPLKNPNGVIQMGLAENQLCLDLIED
WIKRNPKGSICSSFKAIANFQDYHGLPEFRKAIAKFMEKTRGGRVRFDPE
RVVMAGGATGANETIIFCLADPGDAFLVPSPYYPAFNRDLRWRTGVQLIP
IHCESSNNFKITSKAVKEAYENAQKSNIKVKGLILTNPSNPLGTTLDKDT
LKSVLSFTNQHNIHLVCDEIYAATVFDTPQFVSIAEILDEQEMTYCNKDL
VHIVYSLSKDMGLPGFRVGIIYSFNDDVVNCARKMSSFGLVSTQTQYFLA
AMLSDEKFVDNFLRESAMRLGKRHKHFTNGLEVVGIKCLKNNAGLFCWMD
LRPLLRESTFDSEMSLWRVIINDVKLNVSPGSSFECQEPGWFRVCFANMD
DGTVDIALARIRRFVGVEK
3D structure
PDB1iay Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y152 D237 I239 K278
Catalytic site (residue number reindexed from 1) Y133 D218 I220 K259
Enzyme Commision number 4.4.1.14: 1-aminocyclopropane-1-carboxylate synthase.
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 PLP A G126 A127 T128 Y152 Y240 S275 S277 K278 R286 G107 A108 T109 Y133 Y221 S256 S258 K259 R267
BS02 AVG A A54 Y152 A154 A39 Y133 A135
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1iay, PDBe:1iay, PDBj:1iay
PDBsum1iay
PubMed11431475
UniProtP18485|1A12_SOLLC 1-aminocyclopropane-1-carboxylate synthase 2 (Gene Name=ACS2)

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