Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3UZB

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	valine biosynthetic process
A	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
A	0052654	molecular_function	L-leucine transaminase activity
A	0052655	molecular_function	L-valine transaminase activity
A	0052656	molecular_function	L-isoleucine 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	valine biosynthetic process
B	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
B	0052654	molecular_function	L-leucine transaminase activity
B	0052655	molecular_function	L-valine transaminase activity
B	0052656	molecular_function	L-isoleucine transaminase activity
C	0003824	molecular_function	catalytic activity
C	0004084	molecular_function	branched-chain-amino-acid transaminase activity
C	0008483	molecular_function	transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0009081	biological_process	branched-chain amino acid metabolic process
C	0009082	biological_process	branched-chain amino acid biosynthetic process
C	0009097	biological_process	isoleucine biosynthetic process
C	0009098	biological_process	L-leucine biosynthetic process
C	0009099	biological_process	valine biosynthetic process
C	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
C	0052654	molecular_function	L-leucine transaminase activity
C	0052655	molecular_function	L-valine transaminase activity
C	0052656	molecular_function	L-isoleucine transaminase activity
D	0003824	molecular_function	catalytic activity
D	0004084	molecular_function	branched-chain-amino-acid transaminase activity
D	0008483	molecular_function	transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0009081	biological_process	branched-chain amino acid metabolic process
D	0009082	biological_process	branched-chain amino acid biosynthetic process
D	0009097	biological_process	isoleucine biosynthetic process
D	0009098	biological_process	L-leucine biosynthetic process
D	0009099	biological_process	valine biosynthetic process
D	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
D	0052654	molecular_function	L-leucine transaminase activity
D	0052655	molecular_function	L-valine transaminase activity
D	0052656	molecular_function	L-isoleucine 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	ILE266
A	THR267
A	GLY303
A	THR304
A	COI1517
A	LYS202
A	TYR207
A	GLU238
A	GLY240
A	ALA241
A	ALA242
A	ASN243
A	SER265

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE COI A 1517

Chain	Residue
A	PHE76
A	TYR143
A	LYS202
A	ALA241
A	THR304
A	ALA305
A	ALA306
A	PLP371

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP B 372

Chain	Residue
B	ARG100
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	COI2517

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE COI B 2517

Chain	Residue
A	VAL157
B	PHE31
B	TYR143
B	TYR175
B	LYS202
B	ALA241
B	THR304
B	ALA305
B	ALA306
B	HOH367
B	PLP372

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP C 373

Chain	Residue
C	ARG100
C	ARG192
C	LYS202
C	TYR207
C	GLU238
C	GLY240
C	ALA241
C	ALA242
C	ASN243
C	LEU263
C	SER265
C	ILE266
C	THR267
C	GLY303
C	THR304
C	COI3517

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE COI C 3517

Chain	Residue
C	GLY78
C	TYR143
C	TYR175
C	THR304
C	ALA305
C	PLP373
D	VAL157

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP D 374

Chain	Residue
D	ARG100
D	LYS202
D	TYR207
D	GLU238
D	ALA239
D	ALA241
D	ALA242
D	LEU263
D	SER265
D	ILE266
D	THR267
D	GLY303
D	THR304
D	COI4517

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE COI D 4517

Chain	Residue
D	PHE76
D	GLY78
D	TYR143
D	LYS202
D	TYR207
D	ALA241
D	THR304
D	ALA305
D	PLP374

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)