Structure of PDB 1toj Chain A Binding Site BS01

Receptor Information
>1toj Chain A (length=396) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFENITATTADPILGLADLFRADERPGKIDLGIGVYKDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGSGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFAL
YNERVGACTLVAADSETVDRAFGQMKAAIRANYSSPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Ligand information
Ligand IDHCI
InChIInChI=1S/C9H10O2/c10-9(11)7-6-8-4-2-1-3-5-8/h1-5H,6-7H2,(H,10,11)
InChIKeyXMIIGOLPHOKFCH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)CCc1ccccc1
OpenEye OEToolkits 1.7.6c1ccc(cc1)CCC(=O)O
CACTVS 3.370OC(=O)CCc1ccccc1
FormulaC9 H10 O2
NameHYDROCINNAMIC ACID;
3PP;
3-PHENYLPROPIONIC ACID
ChEMBLCHEMBL851
DrugBankDB02024
ZINCZINC000000154564
PDB chain1toj Chain A Residue 410 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1toj Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase
Resolution1.9 Å
Binding residue
(original residue number in PDB)		I17 L18 I37 G38 W140 X258 R386
Binding residue
(residue number reindexed from 1)		I13 L14 I33 G34 W130 X246 R374
Annotation score1
Binding affinityMOAD: Kd=0.41mM
PDBbind-CN: -logKd/Ki=3.39,Kd=0.41mM
Enzymatic activity
Catalytic site (original residue number in PDB) W140 D222 A224 K258
Catalytic site (residue number reindexed from 1) W130 D211 A213 K246
Enzyme Commision number 2.6.1.1: aspartate transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0004838 L-tyrosine-2-oxoglutarate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
GO:0009094 L-phenylalanine biosynthetic process
GO:0033585 L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1toj, PDBe:1toj, PDBj:1toj
PDBsum1toj
PubMed15461450
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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