2ABJ

Crystal structure of human branched chain amino acid transaminase in a complex with an inhibitor, C16H10N2O4F3SCl, and pyridoxal 5' phosphate.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000082	biological_process	G1/S transition of mitotic cell cycle
A	0003824	molecular_function	catalytic activity
A	0004084	molecular_function	branched-chain-amino-acid transaminase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
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	0009098	biological_process	L-leucine biosynthetic process
A	0009099	biological_process	valine biosynthetic process
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
D	0000082	biological_process	G1/S transition of mitotic cell cycle
D	0003824	molecular_function	catalytic activity
D	0004084	molecular_function	branched-chain-amino-acid transaminase activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0008483	molecular_function	transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0009081	biological_process	branched-chain amino acid metabolic process
D	0009082	biological_process	branched-chain amino acid biosynthetic process
D	0009098	biological_process	L-leucine biosynthetic process
D	0009099	biological_process	valine biosynthetic process
D	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
D	0052654	molecular_function	L-leucine transaminase activity
D	0052655	molecular_function	L-valine transaminase activity
D	0052656	molecular_function	L-isoleucine transaminase activity
G	0000082	biological_process	G1/S transition of mitotic cell cycle
G	0003824	molecular_function	catalytic activity
G	0004084	molecular_function	branched-chain-amino-acid transaminase activity
G	0005737	cellular_component	cytoplasm
G	0005739	cellular_component	mitochondrion
G	0005829	cellular_component	cytosol
G	0006629	biological_process	lipid metabolic process
G	0008483	molecular_function	transaminase activity
G	0008652	biological_process	amino acid biosynthetic process
G	0009081	biological_process	branched-chain amino acid metabolic process
G	0009082	biological_process	branched-chain amino acid biosynthetic process
G	0009098	biological_process	L-leucine biosynthetic process
G	0009099	biological_process	valine biosynthetic process
G	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
G	0052654	molecular_function	L-leucine transaminase activity
G	0052655	molecular_function	L-valine transaminase activity
G	0052656	molecular_function	L-isoleucine transaminase activity
J	0000082	biological_process	G1/S transition of mitotic cell cycle
J	0003824	molecular_function	catalytic activity
J	0004084	molecular_function	branched-chain-amino-acid transaminase activity
J	0005737	cellular_component	cytoplasm
J	0005739	cellular_component	mitochondrion
J	0005829	cellular_component	cytosol
J	0006629	biological_process	lipid metabolic process
J	0008483	molecular_function	transaminase activity
J	0008652	biological_process	amino acid biosynthetic process
J	0009081	biological_process	branched-chain amino acid metabolic process
J	0009082	biological_process	branched-chain amino acid biosynthetic process
J	0009098	biological_process	L-leucine biosynthetic process
J	0009099	biological_process	valine biosynthetic process
J	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
J	0052654	molecular_function	L-leucine transaminase activity
J	0052655	molecular_function	L-valine transaminase activity
J	0052656	molecular_function	L-isoleucine transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CBC A 1401

Chain	Residue
A	PHE47
A	THR331
A	ALA332
A	CYS333
A	PLP420
A	HOH1746
A	PHE93
A	TYR159
A	TYR191
A	LYS220
A	GLN242
A	THR258
A	MET259
A	GLY330

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP A 420

Chain	Residue
A	ARG117
A	ARG210
A	LYS220
A	TYR225
A	GLU255
A	THR258
A	ASN260
A	LEU284
A	GLY286
A	VAL287
A	THR288
A	GLY330
A	THR331
A	CBC1401
A	HOH1402
A	HOH1403
A	HOH1404

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CBC D 2401

Chain	Residue
A	VAL173
D	PHE47
D	PHE93
D	TYR159
D	LYS220
D	GLN242
D	THR258
D	MET259
D	GLY330
D	ALA332
D	CYS333
D	PLP420
D	HOH2454

---

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP D 420

Chain	Residue
D	ARG117
D	ARG210
D	LYS220
D	TYR225
D	GLU255
D	THR258
D	MET259
D	ASN260
D	LEU284
D	GLY286
D	VAL287
D	THR288
D	THR331
D	CBC2401
D	HOH2405
D	HOH2408
D	HOH2457

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CBC G 3401

Chain	Residue
G	PHE47
G	PHE93
G	TYR159
G	LYS220
G	GLN242
G	THR258
G	MET259
G	GLY330
G	ALA332
G	CYS333
G	PLP420
G	HOH3444
J	TYR88
J	VAL173

---

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PLP G 420

Chain	Residue
G	ARG117
G	ARG210
G	LYS220
G	TYR225
G	GLU255
G	THR258
G	MET259
G	ASN260
G	LEU284
G	GLY286
G	VAL287
G	THR288
G	GLY330
G	THR331
G	CBC3401
G	HOH3406
G	HOH3407
G	HOH3428

---

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CBC J 4401

Chain	Residue
J	GLN242
J	THR258
J	MET259
J	GLY330
J	THR331
J	ALA332
J	CYS333
J	PLP420
J	HOH4421
G	VAL173
J	PHE47
J	PHE93
J	TYR159
J	TYR191
J	LYS220

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP J 420

Chain	Residue
J	ARG117
J	ARG210
J	LYS220
J	TYR225
J	GLU255
J	THR258
J	ASN260
J	LEU284
J	GLY286
J	VAL287
J	THR288
J	THR331
J	CBC4401
J	HOH4402
J	HOH4403
J	HOH4419

---

Functional Information from PROSITE/UniProt

site_id	PS00770
Number of Residues	35
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EvGtmNLFlywinedgeee.LaTppldgii.LpGVtR

Chain	Residue	Details
A	GLU255-ARG289

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250

Chain	Residue	Details
A	LYS220
D	LYS220
G	LYS220
J	LYS220

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS220

---

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

Chain	Residue	Details
D	LYS220

---

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1iyd

Chain	Residue	Details
G	LYS220

---

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1iyd

Chain	Residue	Details
J	LYS220

---