Structure of PDB 2eiy Chain C

Receptor sequence
>2eiyC (length=294) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
IKAGLIWMNGAFVPQEEAKTSVLSHALHYGTSVFEGIRAYETAKGPAIFR
LKEHVKRFYNSAKVLRMEIPFAPEELEEAIKEVVRRNGYRSCYIRPLAWM
GAKALGVNPLPNNPAEVMVAAWEWKGARLITSSWARFPANVMPGKAKVGG
NYVNSALAKMEAVAAGADEALLLDEEGYVAEGSGENLFFVRDGVIYALEH
SVNLEGITRDSVIRIAKDLGYEVQVVRATRDQLYMADEVFMTGTAAEVTP
VSMIDWRPIGKGTAGPVALRLREVYLEAVTGRRPEYEGWLTYVN
3D structure
PDB2eiy Crystal Structure of T.th.HB8 Branched-Chain Amino Acid Aminotransferase Complexed with 4-Methylvaleric Acid
ChainC
Resolution1.35 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 E193 L216
Catalytic site (residue number reindexed from 1) F34 G36 K147 E181 L204
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 C R59 K159 Y164 E193 G196 E197 L216 G218 I219 T220 G255 T256 R57 K147 Y152 E181 G184 E185 L204 G206 I207 T208 G243 T244
BS02 4MV C Y95 T256 A257 Y93 T244 A245
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0008483 transaminase activity
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: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:0019752 carboxylic acid metabolic process
GO:0046394 carboxylic acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2eiy, PDBe:2eiy, PDBj:2eiy
PDBsum2eiy
PubMed
UniProtQ5SM19

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