3PDB

Crystal structure of mouse mitochondrial aspartate aminotransferase in complex with oxaloacetic acid

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	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005759	cellular_component	mitochondrial matrix
A	0005886	cellular_component	plasma membrane
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0006107	biological_process	oxaloacetate metabolic 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	aspartate catabolic process
A	0006536	biological_process	glutamate metabolic process
A	0006869	biological_process	lipid transport
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0015908	biological_process	fatty acid transport
A	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
A	0019550	biological_process	glutamate catabolic process to aspartate
A	0019551	biological_process	obsolete glutamate catabolic process to 2-oxoglutarate
A	0030170	molecular_function	pyridoxal phosphate binding
A	0043209	cellular_component	myelin sheath
A	0045471	biological_process	response to ethanol
B	0003824	molecular_function	catalytic activity
B	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0005759	cellular_component	mitochondrial matrix
B	0005886	cellular_component	plasma membrane
B	0006103	biological_process	2-oxoglutarate metabolic process
B	0006107	biological_process	oxaloacetate metabolic 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	aspartate catabolic process
B	0006536	biological_process	glutamate metabolic process
B	0006869	biological_process	lipid transport
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0015908	biological_process	fatty acid transport
B	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
B	0019550	biological_process	glutamate catabolic process to aspartate
B	0019551	biological_process	obsolete glutamate catabolic process to 2-oxoglutarate
B	0030170	molecular_function	pyridoxal phosphate binding
B	0043209	cellular_component	myelin sheath
B	0045471	biological_process	response to ethanol
C	0003824	molecular_function	catalytic activity
C	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0005759	cellular_component	mitochondrial matrix
C	0005886	cellular_component	plasma membrane
C	0006103	biological_process	2-oxoglutarate metabolic process
C	0006107	biological_process	oxaloacetate metabolic 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	aspartate catabolic process
C	0006536	biological_process	glutamate metabolic process
C	0006869	biological_process	lipid transport
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0015908	biological_process	fatty acid transport
C	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
C	0019550	biological_process	glutamate catabolic process to aspartate
C	0019551	biological_process	obsolete glutamate catabolic process to 2-oxoglutarate
C	0030170	molecular_function	pyridoxal phosphate binding
C	0043209	cellular_component	myelin sheath
C	0045471	biological_process	response to ethanol
D	0003824	molecular_function	catalytic activity
D	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
D	0005739	cellular_component	mitochondrion
D	0005743	cellular_component	mitochondrial inner membrane
D	0005759	cellular_component	mitochondrial matrix
D	0005886	cellular_component	plasma membrane
D	0006103	biological_process	2-oxoglutarate metabolic process
D	0006107	biological_process	oxaloacetate metabolic 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	aspartate catabolic process
D	0006536	biological_process	glutamate metabolic process
D	0006869	biological_process	lipid transport
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0015908	biological_process	fatty acid transport
D	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
D	0019550	biological_process	glutamate catabolic process to aspartate
D	0019551	biological_process	obsolete glutamate catabolic process to 2-oxoglutarate
D	0030170	molecular_function	pyridoxal phosphate binding
D	0043209	cellular_component	myelin sheath
D	0045471	biological_process	response to ethanol

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME A 1

Chain	Residue
A	TYR67
A	GLU343
A	GLY346
A	MET347

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 431

Chain	Residue
A	ASN91
A	HOH518
B	PRO74
B	VAL76

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 432

Chain	Residue
A	GLY254
A	ASP255
A	ARG262
A	ARG337
A	LEU112

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OAA B 1

Chain	Residue
A	ILE44
A	GLY65
A	TRP162
A	ASN215
A	ARG407
B	ARG313
B	HOH482
B	HOH506

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME B 431

Chain	Residue
B	GLY65
B	LYS279
B	PHE381
B	PMP432

---

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PMP B 432

Chain	Residue
A	TYR96
B	SER133
B	GLY134
B	THR135
B	TRP162
B	ASN215
B	ASP243
B	ALA245
B	TYR246
B	SER276
B	LYS279
B	ARG287
B	BME431
B	HOH625
B	HOH711
B	HOH715

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME B 433

Chain	Residue
B	TYR67
B	TYR75
B	GLU343
B	GLY346

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME C 1

Chain	Residue
C	GLY65
C	TRP162
C	ASN215
C	LLP279
C	PHE381

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME C 431

Chain	Residue
C	TYR67
C	TYR75
C	GLU343
C	GLY346

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 432

Chain	Residue
C	PRO74
C	VAL76
C	ARG81
D	ASN91
D	ASP93

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME D 1

Chain	Residue
D	GLY65
D	TRP162
D	LYS279
D	ARG407
D	PMP432

---

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME D 431

Chain	Residue
D	TYR67
D	ASP69
D	GLY346
D	HOH551
D	HOH558

---

site_id	BC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PMP D 432

Chain	Residue
C	TYR96
D	BME1
D	SER133
D	GLY134
D	THR135
D	LEU138
D	TRP162
D	ASN215
D	ASP243
D	TYR246
D	SER276
D	ALA278
D	LYS279
D	ARG287
D	HOH498
D	HOH712

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 433

Chain	Residue
D	GLU111
D	LEU112
D	ASP255
D	ARG262
D	ARG337
D	LEU341

---

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL D 434

Chain	Residue
D	HIS369
D	GLY385

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	SER276-GLY289
A	SER276-GLY289

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
B	GLY65
B	TRP162
D	GLY65
D	TRP162

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
B	ASN215
B	ARG407
D	ASN215
D	ARG407

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00505

Chain	Residue	Details
B	THR48
D	THR48

---

site_id	SWS_FT_FI4
Number of Residues	14
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753

Chain	Residue	Details
B	LYS59
D	LYS234
D	LYS302
D	LYS345
D	LYS364
D	LYS387
B	LYS82
B	LYS234
B	LYS302
B	LYS345
B	LYS364
B	LYS387
D	LYS59
D	LYS82

---

site_id	SWS_FT_FI5
Number of Residues	24
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337

Chain	Residue	Details
B	LYS73
B	LYS363
B	LYS396
B	LYS404
D	LYS73
D	LYS90
D	LYS107
D	LYS122
D	LYS159
D	LYS185
D	LYS296
B	LYS90
D	LYS309
D	LYS338
D	LYS363
D	LYS396
D	LYS404
B	LYS107
B	LYS122
B	LYS159
B	LYS185
B	LYS296
B	LYS309
B	LYS338

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; alternate => ECO:0000250|UniProtKB:P00505

Chain	Residue	Details
B	TYR96
D	TYR96

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00505

Chain	Residue	Details
B	SER143
D	SER143

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337

Chain	Residue	Details
B	LYS227
D	LYS227

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:23576753

Chain	Residue	Details
B	LYS279
D	LYS279

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Asymmetric dimethylarginine => ECO:0007744|PubMed:24129315

Chain	Residue	Details
B	ARG313
D	ARG313

---