Structure of PDB 2ej2 Chain F

Receptor sequence
>2ej2F (length=298) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
QIKAGLIWMNGAFVPQEEAKTSVLSHALHYGTSVFEGIRAYETAKGPAIF
RLKEHVKRFYNSAKVLRMEIPFAPEELEEAIKEVVRRNGYRSCYIRPLAW
MGAKALGVNPLPNNPAEVMVAAWEWAVRKGARLITSSWARFPANVMPGKA
KVGGNYVNSALAKMEAVAAGADEALLLDEEGYVAEGSGENLFFVRDGVIY
ALEHSVNLEGITRDSVIRIAKDLGYEVQVVRATRDQLYMADEVFMTGTAA
EVTPVSMIDWRPIGKGTAGPVALRLREVYLEAVTGRRPEYEGWLTYVN
3D structure
PDB2ej2 Crystal Structure of T.th.HB8 Branched-Chain Amino Acid Aminotransferase Complexed with N-(5'-Phosphopyridoxyl)-L-Glutamate
ChainF
Resolution2.0 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) F35 G37 K151 E185 L208
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 PPE F R59 Y95 Y164 E193 G196 E197 L216 G218 I219 T220 T256 A257 R58 Y94 Y156 E185 G188 E189 L208 G210 I211 T212 T248 A249
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:2ej2, PDBe:2ej2, PDBj:2ej2
PDBsum2ej2
PubMed
UniProtQ5SM19

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