2HGX

Crystal structure of Cys315Ala mutant of human mitochondrial branched chain aminotransferase

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	L-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	0016740	molecular_function	transferase activity
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	L-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	0016740	molecular_function	transferase activity
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	14
Details	BINDING SITE FOR RESIDUE PLP A 400

Chain	Residue
A	ARG99
A	VAL270
A	THR313
A	HOH1007
A	HOH1029
A	HOH1035
A	ARG192
A	LYS202
A	TYR207
A	GLU237
A	THR240
A	ASN242
A	GLY268
A	VAL269

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 401

Chain	Residue
B	HOH6
B	HOH27
B	HOH29
B	ARG599
B	ARG692
B	LYS702
B	TYR707
B	GLU737
B	THR740
B	ASN742
B	LEU766
B	GLY768
B	VAL769
B	VAL770
B	GLY812
B	THR813
B	ACY1002

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EPE B 1004

Chain	Residue
B	HOH164
B	ASP776
B	MET777
B	THR780
B	TRP781
B	GLU848
B	HIS859

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY A 1001

Chain	Residue
A	HOH1015
A	HOH1130

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY B 1002

Chain	Residue
A	TYR70
B	HOH31
B	PLP401
B	TYR641
B	ARG643

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY B 1003

Chain	Residue
B	ASP630
B	TRP631

---

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 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	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

---

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	LYS702

---