2HDK

Crystal Structure of Cys315Ala-Cys318Ala 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	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
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	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	valine biosynthetic process
B	0010817	biological_process	regulation of hormone levels
B	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
B	0052654	molecular_function	L-leucine transaminase activity
B	0052655	molecular_function	L-valine transaminase activity
B	0052656	molecular_function	L-isoleucine transaminase activity
B	1990830	biological_process	cellular response to leukemia inhibitory factor

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 400

Chain	Residue
A	ARG99
A	VAL270
A	GLY312
A	THR313
A	HOH1002
A	HOH1034
A	HOH1075
A	LYS202
A	TYR207
A	GLU237
A	THR240
A	ASN242
A	LEU266
A	GLY268
A	VAL269

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site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP B 401

Chain	Residue
B	HOH6
B	HOH17
B	HOH86
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

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE COI B 900

Chain	Residue
A	TYR70
A	VAL155
B	HOH63
B	ARG643
B	THR740
B	GLY812
B	THR813
B	ALA814

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

Chain	Residue
A	THR240
A	HOH1039

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12269802, ECO:0000269|PubMed:16141215, ECO:0000269|PubMed:17050531

Chain	Residue	Details
A	TYR141
B	TYR641

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site_id	SWS_FT_FI2
Number of Residues	2
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
B	LYS702

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS294
B	LYS794

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Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS202

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

Chain	Residue	Details
B	LYS702

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