3PD6

Crystal structure of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV

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	0005543	molecular_function	phospholipid binding
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	L-aspartate catabolic process
A	0006536	biological_process	glutamate metabolic process
A	0006538	biological_process	L-glutamate catabolic process
A	0006869	biological_process	lipid transport
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0009986	cellular_component	cell surface
A	0015908	biological_process	fatty acid transport
A	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
A	0016597	molecular_function	amino acid binding
A	0016740	molecular_function	transferase activity
A	0019550	biological_process	L-glutamate catabolic process to aspartate
A	0019899	molecular_function	enzyme binding
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030315	cellular_component	T-tubule
A	0031406	molecular_function	carboxylic acid binding
A	0032991	cellular_component	protein-containing complex
A	0042383	cellular_component	sarcolemma
A	0042802	molecular_function	identical protein binding
A	0043204	cellular_component	perikaryon
A	0043209	cellular_component	myelin sheath
A	0043490	biological_process	malate-aspartate shuttle
A	0045471	biological_process	response to ethanol
B	0003824	molecular_function	catalytic activity
B	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
B	0005543	molecular_function	phospholipid binding
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	L-aspartate catabolic process
B	0006536	biological_process	glutamate metabolic process
B	0006538	biological_process	L-glutamate catabolic process
B	0006869	biological_process	lipid transport
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0009986	cellular_component	cell surface
B	0015908	biological_process	fatty acid transport
B	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
B	0016597	molecular_function	amino acid binding
B	0016740	molecular_function	transferase activity
B	0019550	biological_process	L-glutamate catabolic process to aspartate
B	0019899	molecular_function	enzyme binding
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030315	cellular_component	T-tubule
B	0031406	molecular_function	carboxylic acid binding
B	0032991	cellular_component	protein-containing complex
B	0042383	cellular_component	sarcolemma
B	0042802	molecular_function	identical protein binding
B	0043204	cellular_component	perikaryon
B	0043209	cellular_component	myelin sheath
B	0043490	biological_process	malate-aspartate shuttle
B	0045471	biological_process	response to ethanol
C	0003824	molecular_function	catalytic activity
C	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
C	0005543	molecular_function	phospholipid binding
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	L-aspartate catabolic process
C	0006536	biological_process	glutamate metabolic process
C	0006538	biological_process	L-glutamate catabolic process
C	0006869	biological_process	lipid transport
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0009986	cellular_component	cell surface
C	0015908	biological_process	fatty acid transport
C	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
C	0016597	molecular_function	amino acid binding
C	0016740	molecular_function	transferase activity
C	0019550	biological_process	L-glutamate catabolic process to aspartate
C	0019899	molecular_function	enzyme binding
C	0030170	molecular_function	pyridoxal phosphate binding
C	0030315	cellular_component	T-tubule
C	0031406	molecular_function	carboxylic acid binding
C	0032991	cellular_component	protein-containing complex
C	0042383	cellular_component	sarcolemma
C	0042802	molecular_function	identical protein binding
C	0043204	cellular_component	perikaryon
C	0043209	cellular_component	myelin sheath
C	0043490	biological_process	malate-aspartate shuttle
C	0045471	biological_process	response to ethanol
D	0003824	molecular_function	catalytic activity
D	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
D	0005543	molecular_function	phospholipid binding
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	L-aspartate catabolic process
D	0006536	biological_process	glutamate metabolic process
D	0006538	biological_process	L-glutamate catabolic process
D	0006869	biological_process	lipid transport
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0009986	cellular_component	cell surface
D	0015908	biological_process	fatty acid transport
D	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
D	0016597	molecular_function	amino acid binding
D	0016740	molecular_function	transferase activity
D	0019550	biological_process	L-glutamate catabolic process to aspartate
D	0019899	molecular_function	enzyme binding
D	0030170	molecular_function	pyridoxal phosphate binding
D	0030315	cellular_component	T-tubule
D	0031406	molecular_function	carboxylic acid binding
D	0032991	cellular_component	protein-containing complex
D	0042383	cellular_component	sarcolemma
D	0042802	molecular_function	identical protein binding
D	0043204	cellular_component	perikaryon
D	0043209	cellular_component	myelin sheath
D	0043490	biological_process	malate-aspartate shuttle
D	0045471	biological_process	response to ethanol

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PMP A 1

Chain	Residue
A	SER133
A	ARG287
A	HOH678
A	HOH785
B	KYN1
B	TYR96
A	GLY134
A	THR135
A	TRP162
A	ASN215
A	ASP243
A	TYR246
A	SER276
A	LYS279

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 431

Chain	Residue
A	TYR67
A	ASP69
A	TYR75
A	GLU343
A	GLY346
A	HOH571

---

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

Chain	Residue
A	ASN370
A	TRP371
A	HIS373
A	THR384
A	HOH563

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 433

Chain	Residue
A	GLN204
A	ASN237
B	SER30
B	TRP32

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE KYN B 1

Chain	Residue
A	PMP1
A	ILE44
A	TRP162
A	PHE381
A	ARG407
B	TYR96
B	ARG313
B	SER317
B	ASN318

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 431

Chain	Residue
A	ARG313
B	TRP162
B	ASN215
B	PHE381
B	ARG407

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 432

Chain	Residue
B	TYR67
B	ASP69
B	GLY346
B	MET347
B	HOH701

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 433

Chain	Residue
A	SER30
A	SER31
A	TRP32
B	GLN204
B	ASN237

---

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PMP C 1

Chain	Residue
C	SER133
C	GLY134
C	THR135
C	TRP162
C	ASN215
C	ASP243
C	TYR246
C	SER276
C	LYS279
C	ARG287
C	GOL433
C	HOH786
C	HOH787
D	TYR96

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 431

Chain	Residue
C	TYR67
C	ASP69
C	ASP70
C	GLY346
C	MET347
C	ARG350
C	HOH566

---

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 432

Chain	Residue
C	LEU157
C	PRO158
C	PRO160
C	SER161
C	TRP162
C	GLY163
C	THR166
C	HOH784

---

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 433

Chain	Residue
C	PMP1
C	GLY65
C	TRP162
C	ASN215
C	LYS279
C	PHE381
C	ARG407
D	ARG313

---

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 434

Chain	Residue
C	ASN91
D	PRO74
D	VAL76
D	ARG81

---

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 435

Chain	Residue
C	SER30
C	SER31
D	GLN204
D	ASN237

---

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 436

Chain	Residue
C	HOH805
D	SER31
C	ASN237

---

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1

Chain	Residue
D	TYR67
D	ASP69
D	ASP70
D	TYR75
D	GLY346
D	ARG350

---

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
A	SER276-GLY289
B	SER276-GLY289

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00505","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	28
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	48
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine; alternate","evidences":[{"source":"UniProtKB","id":"P00505","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00505","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Asymmetric dimethylarginine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---