Structure of PDB 1iyd Chain A

Receptor sequence
>1iydA (length=304) Species: 562 (Escherichia coli) [Search protein sequence]
KADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRH
REHMQRLHDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLIFVG
DVGMGVNPPAGYSTDVIIAAFPWGAYLGAEALEQGIDAMVSSWNRAAPNT
IPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVK
DGVLFTPPFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVF
MSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWL
DQVN
3D structure
PDB1iyd Crystal structures of branched-chain amino Acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 R59 K159 Y164 E193 G196 E197 L217 G219 I220 T221 T257 R56 K156 Y161 E190 G193 E194 L214 G216 I217 T218 T254
BS02 GUA A Y95 Y129 A258 Y92 Y126 A255
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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