3UYY

Crystal Structures of Branched-Chain Aminotransferase from Deinococcus radiodurans Complexes with alpha-Ketoisocaproate and L-Glutamate Suggest Its Radio-Resistance for Catalysis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004084	molecular_function	branched-chain-amino-acid transaminase activity
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009081	biological_process	branched-chain amino acid metabolic process
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009097	biological_process	isoleucine biosynthetic process
A	0009098	biological_process	L-leucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0052654	molecular_function	L-leucine-2-oxoglutarate transaminase activity
A	0052655	molecular_function	L-valine-2-oxoglutarate transaminase activity
A	0052656	molecular_function	L-isoleucine-2-oxoglutarate transaminase activity
B	0003824	molecular_function	catalytic activity
B	0004084	molecular_function	branched-chain-amino-acid transaminase activity
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009081	biological_process	branched-chain amino acid metabolic process
B	0009082	biological_process	branched-chain amino acid biosynthetic process
B	0009097	biological_process	isoleucine biosynthetic process
B	0009098	biological_process	L-leucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0052654	molecular_function	L-leucine-2-oxoglutarate transaminase activity
B	0052655	molecular_function	L-valine-2-oxoglutarate transaminase activity
B	0052656	molecular_function	L-isoleucine-2-oxoglutarate transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 371

Chain	Residue
A	ARG100
A	SER265
A	ILE266
A	THR267
A	THR304
A	HOH377
A	ARG192
A	LYS202
A	TYR207
A	GLU238
A	GLY240
A	ALA241
A	ALA242
A	LEU263

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site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP B 372

Chain	Residue
B	ARG100
B	ARG192
B	LYS202
B	TYR207
B	GLU238
B	GLY240
B	ALA241
B	ALA242
B	LEU263
B	SER265
B	ILE266
B	THR267
B	GLY303
B	THR304
B	HOH404

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Functional Information from PROSITE/UniProt

site_id	PS00770
Number of Residues	31
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EaGaaNFFaitqdgqk....FvTpqspsi..LpSItK

Chain	Residue	Details
A	GLU238-LYS268

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