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	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
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	0016740	molecular_function	transferase activity
A	0050873	biological_process	brown fat cell differentiation
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	0097009	biological_process	energy homeostasis

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 site: {"evidences":[{"source":"PubMed","id":"12269802","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16141215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17050531","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"16141215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17050531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HG8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HGX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HHF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---