Structure of PDB 2ej2 Chain D

Receptor sequence

>2ej2D (length=301) Species: 300852 (Thermus thermophilus HB8)

QIKAGLIWMNGAFVPQEEAKTSVLSHALHYGTSVFEGIRAYETAKGPAIF
RLKEHVKRFYNSAKVLRMEIPFAPEELEEAIKEVVRRNGYRSCYIRPLAW
MGAKALGVNPLPNNPAEVMVAAWEWGAYLVRKGARLITSSWARFPANVMP
GKAKVGGNYVNSALAKMEAVAAGADEALLLDEEGYVAEGSGENLFFVRDG
VIYALEHSVNLEGITRDSVIRIAKDLGYEVQVVRATRDQLYMADEVFMTG
TAAEVTPVSMIDWRPIGKGTAGPVALRLREVYLEAVTGRRPEYEGWLTYV
N

3D structure

• PDB: 2ej2 Crystal Structure of T.th.HB8 Branched-Chain Amino Acid Aminotransferase Complexed with N-(5'-Phosphopyridoxyl)-L-Glutamate
• Chain: D
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F36 G38 K159 E193 L216
• Catalytic site (residue number reindexed from 1): F35 G37 K154 E188 L211
• 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	D	R59 Y95 Y164 E193 G196 E197 L216 G218 I219 T220 G255 T256 A257	R58 Y94 Y159 E188 G191 E192 L211 G213 I214 T215 G250 T251 A252

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

External links

• PDB: RCSB:2ej2, PDBe:2ej2, PDBj:2ej2
• PDBsum: 2ej2
• UniProt: Q5SM19