Structure of PDB 1yoo Chain A Binding Site BS02

Receptor Information
>1yoo 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]
MFENITTAPADPILGLADLLRADERPGKIDLGMGVYNDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVRRVWVSNPGWPTHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGTCTLVAADSETVDRAFSQMKAAIRVNYSSPPAHGASVVATILGN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFTIKQNGMFFF
GGLTKEQVLRLREEFGVYAVASGRLNVAGMTPDNLAPLCEAIVAVL
Ligand information
Ligand IDIVA
InChIInChI=1S/C5H10O2/c1-4(2)3-5(6)7/h4H,3H2,1-2H3,(H,6,7)
InChIKeyGWYFCOCPABKNJV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0CC(C)CC(=O)O
CACTVS 3.370CC(C)CC(O)=O
ACDLabs 12.01O=C(O)CC(C)C
FormulaC5 H10 O2
NameISOVALERIC ACID
ChEMBLCHEMBL568737
DrugBankDB03750
ZINCZINC000000388188
PDB chain1yoo Chain A Residue 414 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1yoo Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		G38 W140 R386
Binding residue
(residue number reindexed from 1)		G34 W130 R374
Annotation score2
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:1yoo, PDBe:1yoo, PDBj:1yoo
PDBsum1yoo
PubMed9891001
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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