Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HLM

Crystal Structure of Mouse Mitochondrial Aspartate Aminotransferase/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	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	0015908	biological_process	fatty acid transport
A	0016020	cellular_component	membrane
A	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
A	0016740	molecular_function	transferase activity
A	0019550	biological_process	L-glutamate catabolic process to aspartate
A	0030170	molecular_function	pyridoxal phosphate binding
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	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	0015908	biological_process	fatty acid transport
B	0016020	cellular_component	membrane
B	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
B	0016740	molecular_function	transferase activity
B	0019550	biological_process	L-glutamate catabolic process to aspartate
B	0030170	molecular_function	pyridoxal phosphate binding
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	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	0015908	biological_process	fatty acid transport
C	0016020	cellular_component	membrane
C	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
C	0016740	molecular_function	transferase activity
C	0019550	biological_process	L-glutamate catabolic process to aspartate
C	0030170	molecular_function	pyridoxal phosphate binding
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	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	0015908	biological_process	fatty acid transport
D	0016020	cellular_component	membrane
D	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
D	0016740	molecular_function	transferase activity
D	0019550	biological_process	L-glutamate catabolic process to aspartate
D	0030170	molecular_function	pyridoxal phosphate binding
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	7
Details	BINDING SITE FOR RESIDUE GOL A 1

Chain	Residue
A	ILE44
A	TRP162
A	GLY163
A	ASN215
A	ARG407
A	HOH565
B	ARG313

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 431

Chain	Residue
A	TYR75
A	GLY346
A	MET347
A	TYR67
A	ASP69

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 432

Chain	Residue
A	SER143
A	GLN146
A	ARG147
A	ALA172
A	HOH446
A	HOH467
A	HOH478
B	ASP171

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1

Chain	Residue
B	TYR67
B	ASP69
B	GLY346
B	HOH521

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 431

Chain	Residue
A	ARG170
A	ASP171
B	ARG147
B	ILE310
B	HOH432
B	HOH433
B	HOH482

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1

Chain	Residue
C	TRP162
C	GLY163
C	ASN164
C	HOH535
D	ARG313

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

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

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