5CM0

Crystal structure of branched-chain aminotransferase from thermophilic archaea Geoglobus acetivorans

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	0019752	biological_process	carboxylic acid metabolic process
A	0046394	biological_process	carboxylic acid biosynthetic process
A	0050048	molecular_function	obsolete L-leucine:2-oxoglutarate aminotransferase 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	0019752	biological_process	carboxylic acid metabolic process
B	0046394	biological_process	carboxylic acid biosynthetic process
B	0050048	molecular_function	obsolete L-leucine:2-oxoglutarate aminotransferase 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
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	L-valine biosynthetic process
C	0019752	biological_process	carboxylic acid metabolic process
C	0046394	biological_process	carboxylic acid biosynthetic process
C	0050048	molecular_function	obsolete L-leucine:2-oxoglutarate aminotransferase activity
C	0052654	molecular_function	L-leucine-2-oxoglutarate transaminase activity
C	0052655	molecular_function	L-valine-2-oxoglutarate transaminase activity
C	0052656	molecular_function	L-isoleucine-2-oxoglutarate transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue PLP A 301

Chain	Residue
A	HIS50
A	ASP189
A	ASN190
A	LEU208
A	ILE211
A	THR212
A	GLY247
A	THR248
A	HOH430
A	HOH473
A	ARG53
A	ARG141
A	LYS152
A	TYR156
A	ASN159
A	GLU185
A	SER187
A	GLY188

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site_id	AC2
Number of Residues	3
Details	binding site for residue GOL A 302

Chain	Residue
A	GLU129
A	LYS130
A	PRO268

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site_id	AC3
Number of Residues	3
Details	binding site for residue GOL C 302

Chain	Residue
C	LYS130
C	HOH412
C	HOH546

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site_id	AC4
Number of Residues	20
Details	binding site for residue PLP B 301

Chain	Residue
B	VAL33
B	PHE34
B	ARG53
B	CYS57
B	ARG141
B	ASN150
B	ILE151
B	SER153
B	TYR156
B	ASN159
B	GLU185
B	GLY188
B	ASP189
B	GLY210
B	ILE211
B	THR212
B	GLY247
B	THR248
B	HOH428
B	HOH463

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site_id	AC5
Number of Residues	20
Details	binding site for residue PLP C 301

Chain	Residue
C	VAL33
C	PHE34
C	ARG53
C	CYS57
C	ARG141
C	ASN150
C	ILE151
C	SER153
C	TYR156
C	ASN159
C	GLU185
C	SER187
C	GLY188
C	GLY210
C	ILE211
C	THR212
C	GLY247
C	THR248
C	HOH426
C	HOH444

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Functional Information from PROSITE/UniProt

site_id	PS00770
Number of Residues	29
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSgdNIFivkngt......ItTpptlnn..LkGItR

Chain	Residue	Details
A	GLU185-ARG213

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