6PRX

oxidized Human Branched Chain Aminotransferase mutant C318A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004084	molecular_function	branched-chain-amino-acid:2-oxoglutarate transaminase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006550	biological_process	L-isoleucine catabolic process
A	0006552	biological_process	L-leucine catabolic process
A	0006574	biological_process	L-valine catabolic 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	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
A	1903444	biological_process	negative regulation of brown fat cell differentiation
B	0003824	molecular_function	catalytic activity
B	0004084	molecular_function	branched-chain-amino-acid:2-oxoglutarate transaminase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006550	biological_process	L-isoleucine catabolic process
B	0006552	biological_process	L-leucine catabolic process
B	0006574	biological_process	L-valine catabolic 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	0050873	biological_process	brown fat cell differentiation
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	0097009	biological_process	energy homeostasis
B	1903444	biological_process	negative regulation of brown fat cell differentiation

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue PLP A 401

Chain	Residue
A	ARG99
A	LEU266
A	GLY268
A	VAL269
A	VAL270
A	GLY312
A	THR313
A	ARG192
A	LYS202
A	TYR207
A	GLU237
A	GLY239
A	THR240
A	MET241
A	ASN242

---

site_id	AC2
Number of Residues	15
Details	binding site for Di-peptide PLP B 400 and LYS B 202

Chain	Residue
B	PHE75
B	SER103
B	TYR201
B	LEU203
B	TYR207
B	GLU237
B	THR240
B	MET241
B	ASN242
B	LEU266
B	GLY268
B	VAL269
B	VAL270
B	GLY312
B	THR313

---

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	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12269802","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
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	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---