Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1EKV

HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL): THREE DIMENSIONAL STRUCTURE OF ENZYME INACTIVATED BY TRIS BOUND TO THE PYRIDOXAL-5'-PHOSPHATE ON ONE END AND ACTIVE SITE LYS202 NZ ON THE OTHER.

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	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006549	biological_process	isoleucine metabolic process
A	0006550	biological_process	isoleucine catabolic process
A	0006551	biological_process	L-leucine metabolic process
A	0006573	biological_process	valine metabolic process
A	0006629	biological_process	lipid metabolic process
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	0009083	biological_process	branched-chain amino acid catabolic process
A	0009098	biological_process	L-leucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0010817	biological_process	regulation of hormone levels
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
A	1990830	biological_process	cellular response to leukemia inhibitory factor
B	0003824	molecular_function	catalytic activity
B	0004084	molecular_function	branched-chain-amino-acid transaminase activity
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006549	biological_process	isoleucine metabolic process
B	0006550	biological_process	isoleucine catabolic process
B	0006551	biological_process	L-leucine metabolic process
B	0006573	biological_process	valine metabolic process
B	0006629	biological_process	lipid metabolic process
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	0009083	biological_process	branched-chain amino acid catabolic process
B	0009098	biological_process	L-leucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0010817	biological_process	regulation of hormone levels
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
B	1990830	biological_process	cellular response to leukemia inhibitory factor

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 370

Chain	Residue
A	ARG99
A	VAL269
A	VAL270
A	GLY312
A	THR313
A	TRS371
A	HOH395
A	ARG192
A	TYR207
A	GLU237
A	GLY239
A	THR240
A	ASN242
A	LEU266
A	GLY268

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 370

Chain	Residue
B	ARG99
B	ARG192
B	TYR207
B	GLU237
B	GLY239
B	THR240
B	MET241
B	ASN242
B	LEU266
B	GLY268
B	VAL269
B	VAL270
B	GLY312
B	THR313
B	TRS371
B	HOH376
B	HOH410

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TRS A 371

Chain	Residue
A	PHE75
A	TYR141
A	LYS202
A	TYR207
A	PLP370
A	HOH395

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS B 371

Chain	Residue
B	PHE75
B	LYS202
B	TYR207
B	THR240
B	PLP370
B	HOH410
B	HOH414

Functional Information from PROSITE/UniProt

site_id	PS00770
Number of Residues	35
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EvGtmNIFvywthedgvle.LvTpplngvi.LpGVvR

Chain	Residue	Details
A	GLU237-ARG271

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:12269802, ECO:0000269\|PubMed:16141215, ECO:0000269\|PubMed:17050531

Chain	Residue	Details
A	TYR141
B	TYR141

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:16141215, ECO:0000269\|PubMed:17050531, ECO:0007744\|PDB:2A1H, ECO:0007744\|PDB:2HDK, ECO:0007744\|PDB:2HG8, ECO:0007744\|PDB:2HGW, ECO:0007744\|PDB:2HGX, ECO:0007744\|PDB:2HHF

Chain	Residue	Details
A	LYS202
B	LYS202

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS294
B	LYS294

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1iyd

Chain	Residue	Details
A	LYS202

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1iyd

Chain	Residue	Details
B	LYS202

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