Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3II0

Crystal structure of human Glutamate oxaloacetate transaminase 1 (GOT1)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0004609	molecular_function	phosphatidylserine decarboxylase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0006107	biological_process	oxaloacetate metabolic process
A	0006114	biological_process	glycerol biosynthetic process
A	0006520	biological_process	amino acid metabolic process
A	0006531	biological_process	aspartate metabolic process
A	0006532	biological_process	aspartate biosynthetic process
A	0006533	biological_process	L-aspartate catabolic process
A	0006536	biological_process	glutamate metabolic process
A	0007219	biological_process	Notch signaling pathway
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009058	biological_process	biosynthetic process
A	0009743	biological_process	response to carbohydrate
A	0016740	molecular_function	transferase activity
A	0019550	biological_process	L-glutamate catabolic process to aspartate
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030511	biological_process	positive regulation of transforming growth factor beta receptor signaling pathway
A	0031406	molecular_function	carboxylic acid binding
A	0032869	biological_process	cellular response to insulin stimulus
A	0032966	biological_process	negative regulation of collagen biosynthetic process
A	0035902	biological_process	response to immobilization stress
A	0043490	biological_process	malate-aspartate shuttle
A	0043648	biological_process	dicarboxylic acid metabolic process
A	0043679	cellular_component	axon terminus
A	0046686	biological_process	response to cadmium ion
A	0047801	molecular_function	L-cysteine transaminase activity
A	0051384	biological_process	response to glucocorticoid
A	0051481	biological_process	negative regulation of cytosolic calcium ion concentration
A	0051902	biological_process	negative regulation of mitochondrial depolarization
A	0055089	biological_process	fatty acid homeostasis
A	0060290	biological_process	transdifferentiation
A	0070062	cellular_component	extracellular exosome
A	0071260	biological_process	cellular response to mechanical stimulus
A	0097054	biological_process	L-glutamate biosynthetic process
A	1990267	biological_process	response to transition metal nanoparticle
B	0003824	molecular_function	catalytic activity
B	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
B	0004609	molecular_function	phosphatidylserine decarboxylase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006103	biological_process	2-oxoglutarate metabolic process
B	0006107	biological_process	oxaloacetate metabolic process
B	0006114	biological_process	glycerol biosynthetic process
B	0006520	biological_process	amino acid metabolic process
B	0006531	biological_process	aspartate metabolic process
B	0006532	biological_process	aspartate biosynthetic process
B	0006533	biological_process	L-aspartate catabolic process
B	0006536	biological_process	glutamate metabolic process
B	0007219	biological_process	Notch signaling pathway
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009058	biological_process	biosynthetic process
B	0009743	biological_process	response to carbohydrate
B	0016740	molecular_function	transferase activity
B	0019550	biological_process	L-glutamate catabolic process to aspartate
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030511	biological_process	positive regulation of transforming growth factor beta receptor signaling pathway
B	0031406	molecular_function	carboxylic acid binding
B	0032869	biological_process	cellular response to insulin stimulus
B	0032966	biological_process	negative regulation of collagen biosynthetic process
B	0035902	biological_process	response to immobilization stress
B	0043490	biological_process	malate-aspartate shuttle
B	0043648	biological_process	dicarboxylic acid metabolic process
B	0043679	cellular_component	axon terminus
B	0046686	biological_process	response to cadmium ion
B	0047801	molecular_function	L-cysteine transaminase activity
B	0051384	biological_process	response to glucocorticoid
B	0051481	biological_process	negative regulation of cytosolic calcium ion concentration
B	0051902	biological_process	negative regulation of mitochondrial depolarization
B	0055089	biological_process	fatty acid homeostasis
B	0060290	biological_process	transdifferentiation
B	0070062	cellular_component	extracellular exosome
B	0071260	biological_process	cellular response to mechanical stimulus
B	0097054	biological_process	L-glutamate biosynthetic process
B	1990267	biological_process	response to transition metal nanoparticle
C	0003824	molecular_function	catalytic activity
C	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
C	0004609	molecular_function	phosphatidylserine decarboxylase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0006103	biological_process	2-oxoglutarate metabolic process
C	0006107	biological_process	oxaloacetate metabolic process
C	0006114	biological_process	glycerol biosynthetic process
C	0006520	biological_process	amino acid metabolic process
C	0006531	biological_process	aspartate metabolic process
C	0006532	biological_process	aspartate biosynthetic process
C	0006533	biological_process	L-aspartate catabolic process
C	0006536	biological_process	glutamate metabolic process
C	0007219	biological_process	Notch signaling pathway
C	0008483	molecular_function	transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0009058	biological_process	biosynthetic process
C	0009743	biological_process	response to carbohydrate
C	0016740	molecular_function	transferase activity
C	0019550	biological_process	L-glutamate catabolic process to aspartate
C	0030170	molecular_function	pyridoxal phosphate binding
C	0030511	biological_process	positive regulation of transforming growth factor beta receptor signaling pathway
C	0031406	molecular_function	carboxylic acid binding
C	0032869	biological_process	cellular response to insulin stimulus
C	0032966	biological_process	negative regulation of collagen biosynthetic process
C	0035902	biological_process	response to immobilization stress
C	0043490	biological_process	malate-aspartate shuttle
C	0043648	biological_process	dicarboxylic acid metabolic process
C	0043679	cellular_component	axon terminus
C	0046686	biological_process	response to cadmium ion
C	0047801	molecular_function	L-cysteine transaminase activity
C	0051384	biological_process	response to glucocorticoid
C	0051481	biological_process	negative regulation of cytosolic calcium ion concentration
C	0051902	biological_process	negative regulation of mitochondrial depolarization
C	0055089	biological_process	fatty acid homeostasis
C	0060290	biological_process	transdifferentiation
C	0070062	cellular_component	extracellular exosome
C	0071260	biological_process	cellular response to mechanical stimulus
C	0097054	biological_process	L-glutamate biosynthetic process
C	1990267	biological_process	response to transition metal nanoparticle
D	0003824	molecular_function	catalytic activity
D	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
D	0004609	molecular_function	phosphatidylserine decarboxylase activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006103	biological_process	2-oxoglutarate metabolic process
D	0006107	biological_process	oxaloacetate metabolic process
D	0006114	biological_process	glycerol biosynthetic process
D	0006520	biological_process	amino acid metabolic process
D	0006531	biological_process	aspartate metabolic process
D	0006532	biological_process	aspartate biosynthetic process
D	0006533	biological_process	L-aspartate catabolic process
D	0006536	biological_process	glutamate metabolic process
D	0007219	biological_process	Notch signaling pathway
D	0008483	molecular_function	transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0009058	biological_process	biosynthetic process
D	0009743	biological_process	response to carbohydrate
D	0016740	molecular_function	transferase activity
D	0019550	biological_process	L-glutamate catabolic process to aspartate
D	0030170	molecular_function	pyridoxal phosphate binding
D	0030511	biological_process	positive regulation of transforming growth factor beta receptor signaling pathway
D	0031406	molecular_function	carboxylic acid binding
D	0032869	biological_process	cellular response to insulin stimulus
D	0032966	biological_process	negative regulation of collagen biosynthetic process
D	0035902	biological_process	response to immobilization stress
D	0043490	biological_process	malate-aspartate shuttle
D	0043648	biological_process	dicarboxylic acid metabolic process
D	0043679	cellular_component	axon terminus
D	0046686	biological_process	response to cadmium ion
D	0047801	molecular_function	L-cysteine transaminase activity
D	0051384	biological_process	response to glucocorticoid
D	0051481	biological_process	negative regulation of cytosolic calcium ion concentration
D	0051902	biological_process	negative regulation of mitochondrial depolarization
D	0055089	biological_process	fatty acid homeostasis
D	0060290	biological_process	transdifferentiation
D	0070062	cellular_component	extracellular exosome
D	0071260	biological_process	cellular response to mechanical stimulus
D	0097054	biological_process	L-glutamate biosynthetic process
D	1990267	biological_process	response to transition metal nanoparticle

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 1

Chain	Residue
A	GLY108
A	SER258
A	LYS259
A	ARG267
A	TAR435
A	HOH445
D	TYR71
A	GLY109
A	THR110
A	TRP141
A	ASN195
A	ASP223
A	ALA225
A	TYR226
A	SER256

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TAR A 435

Chain	Residue
A	PLP1
A	VAL18
A	PHE19
A	VAL38
A	GLY39
A	TRP141
A	ASN195
A	TYR226
A	LYS259
A	PHE361
A	ARG387
A	HOH445
A	HOH548
D	TYR71
D	ARG293

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 3

Chain	Residue
A	ASN128
A	LYS130
A	HOH438
C	EDO7

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 11

Chain	Residue
A	TYR41
A	THR43
A	TRP49
A	HOH455
A	HOH500

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 436

Chain	Residue
A	ALA78
A	ARG81
A	SER82
A	SER85
A	GLY102
A	GLY103
A	HOH475

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP B 2

Chain	Residue
B	GLY108
B	GLY109
B	THR110
B	TRP141
B	ASN195
B	ASP223
B	ALA225
B	TYR226
B	SER256
B	SER258
B	LYS259
B	ARG267
B	TAR435
B	HOH483
C	TYR71

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TAR B 435

Chain	Residue
B	PLP2
B	VAL18
B	PHE19
B	VAL38
B	GLY39
B	TRP141
B	ASN195
B	TYR226
B	LYS259
B	ARG387
B	HOH483
B	HOH576
C	TYR71
C	ARG293

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 1

Chain	Residue
B	TYR41
B	THR43
B	TRP49
B	HOH551

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 10

Chain	Residue
B	ASN128
B	LYS130
B	HOH470
D	EDO6

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 436

Chain	Residue
B	ALA78
B	ARG81
B	SER82
B	GLY103
B	HOH510
B	HOH696

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP C 3

Chain	Residue
C	SER258
C	LYS259
C	ARG267
C	TAR435
B	TYR71
B	HOH462
C	GLY108
C	GLY109
C	THR110
C	TRP141
C	ASN195
C	ASP223
C	TYR226
C	SER256

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TAR C 435

Chain	Residue
B	TYR71
B	ARG293
B	HOH462
C	PLP3
C	VAL18
C	PHE19
C	VAL38
C	GLY39
C	TRP141
C	ASN195
C	TYR226
C	LYS259
C	PHE361
C	ARG387
C	HOH527

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 5

Chain	Residue
A	LEU416
C	TYR124
C	ASN125

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 7

Chain	Residue
A	EDO3
C	ARG157
C	SER158

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 12

Chain	Residue
C	TYR41
C	THR326
C	HOH704

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 436

Chain	Residue
C	ARG81
C	GLY103
C	HOH467
C	HOH468

site_id	BC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP D 4

Chain	Residue
A	TYR71
A	HOH458
D	GLY108
D	GLY109
D	THR110
D	TRP141
D	ASN195
D	ASP223
D	TYR226
D	SER256
D	SER258
D	LYS259
D	ARG267
D	TAR435

site_id	BC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TAR D 435

Chain	Residue
A	TYR71
A	ARG293
A	HOH458
D	PLP4
D	VAL18
D	PHE19
D	GLY39
D	TRP141
D	ASN195
D	TYR226
D	LYS259
D	PHE361
D	ARG387
D	HOH521

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 6

Chain	Residue
B	EDO10
D	ARG157
D	SER158

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 8

Chain	Residue
D	TYR41
D	THR43
D	TRP49
D	HOH497

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 9

Chain	Residue
D	ARG81
D	SER85
D	VAL101
D	HOH535
D	HOH551

Functional Information from PROSITE/UniProt

site_id	PS00105
Number of Residues	14
Details	AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKnfGLyNERVG

Chain	Residue	Details
A	SER256-GLY269

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13221","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	LYS259
A	ASP223
A	TRP141

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	LYS259
B	ASP223
B	TRP141

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	LYS259
C	ASP223
C	TRP141

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	LYS259
D	ASP223
D	TRP141

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	ASP223
A	TRP141

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	ASP223
B	TRP141

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	ASP223
C	TRP141

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	ASP223
D	TRP141

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)