Structure of PDB 1iyd Chain A Binding Site BS02

Receptor Information
>1iyd Chain A (length=304) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRH
REHMQRLHDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLIFVG
DVGMGVNPPAGYSTDVIIAAFPWGAYLGAEALEQGIDAMVSSWNRAAPNT
IPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVK
DGVLFTPPFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVF
MSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWL
DQVN
Ligand information
Ligand IDGUA
InChIInChI=1S/C5H8O4/c6-4(7)2-1-3-5(8)9/h1-3H2,(H,6,7)(H,8,9)
InChIKeyJFCQEDHGNNZCLN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CC(=O)O)CC(=O)O
ACDLabs 10.04O=C(O)CCCC(=O)O
CACTVS 3.341OC(=O)CCCC(O)=O
FormulaC5 H8 O4
NameGLUTARIC ACID
ChEMBLCHEMBL1162495
DrugBankDB03553
ZINCZINC000000388706
PDB chain1iyd 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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PDB1iyd Crystal structures of branched-chain amino Acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme.
Resolution2.15 Å
Binding residue
(original residue number in PDB)		Y95 Y129 A258
Binding residue
(residue number reindexed from 1)		Y92 Y126 A255
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) F36 G38 K159 A160 E193 L217
Catalytic site (residue number reindexed from 1) F33 G35 K156 A157 E190 L214
Enzyme Commision number 2.6.1.42: branched-chain-amino-acid transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0008483 transaminase activity
GO:0042802 identical protein binding
GO:0052654 L-leucine-2-oxoglutarate transaminase activity
GO:0052655 L-valine-2-oxoglutarate transaminase activity
GO:0052656 L-isoleucine-2-oxoglutarate transaminase activity
Biological Process
GO:0006532 aspartate biosynthetic process
GO:0008652 amino acid biosynthetic process
GO:0009081 branched-chain amino acid metabolic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009097 isoleucine biosynthetic process
GO:0009098 L-leucine biosynthetic process
GO:0009099 L-valine biosynthetic process
GO:0046394 carboxylic acid biosynthetic process
Cellular Component
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:1iyd, PDBe:1iyd, PDBj:1iyd
PDBsum1iyd
PubMed12667063
UniProtP0AB80|ILVE_ECOLI Branched-chain-amino-acid aminotransferase (Gene Name=ilvE)

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