5MPR

Single Amino Acid Variant of Human Mitochondrial Branched Chain Amino Acid Aminotransferase 2

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	valine biosynthetic process
A	0010817	biological_process	regulation of hormone levels
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
A	1990830	biological_process	cellular response to leukemia inhibitory factor

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue PLP A 401

Chain	Residue
A	ARG99
A	VAL269
A	VAL270
A	GLY312
A	THR313
A	EDO405
A	HOH541
A	HOH581
A	HOH588
A	ARG192
A	LYS202
A	TYR207
A	GLU237
A	THR240
A	ASN242
A	LEU266
A	GLY268

---

site_id	AC2
Number of Residues	5
Details	binding site for residue EDO A 402

Chain	Residue
A	TYR246
A	ARG306
A	LEU341
A	ARG344
A	HOH503

---

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO A 403

Chain	Residue
A	ASP276
A	MET277
A	THR280
A	HIS359

---

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO A 404

Chain	Residue
A	GLU42
A	LEU59
A	THR60
A	LEU162

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO A 405

Chain	Residue
A	TYR70
A	ARG143
A	LYS202
A	PLP401

---

site_id	AC6
Number of Residues	6
Details	binding site for residue EDO A 406

Chain	Residue
A	THR15
A	LYS17
A	HIS19
A	ASP36
A	PHE56
A	HOH620

---

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	1
Details	BINDING: BINDING => ECO:0000269|PubMed:12269802, ECO:0000269|PubMed:16141215, ECO:0000269|PubMed:17050531

Chain	Residue	Details
A	TYR141

---

site_id	SWS_FT_FI2
Number of Residues	1
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

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS294

---