Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5AX8

Recombinant expression, purification and preliminary crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003824	molecular_function	catalytic activity
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005886	cellular_component	plasma membrane
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0006520	biological_process	amino acid metabolic process
A	0006531	biological_process	aspartate metabolic process
A	0006533	biological_process	L-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	0016740	molecular_function	transferase activity
A	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0043490	biological_process	malate-aspartate shuttle
A	0045471	biological_process	response to ethanol
A	0070062	cellular_component	extracellular exosome
B	0003723	molecular_function	RNA binding
B	0003824	molecular_function	catalytic activity
B	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005886	cellular_component	plasma membrane
B	0006103	biological_process	2-oxoglutarate metabolic process
B	0006520	biological_process	amino acid metabolic process
B	0006531	biological_process	aspartate metabolic process
B	0006533	biological_process	L-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	0016740	molecular_function	transferase activity
B	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0043490	biological_process	malate-aspartate shuttle
B	0045471	biological_process	response to ethanol
B	0070062	cellular_component	extracellular exosome
C	0003723	molecular_function	RNA binding
C	0003824	molecular_function	catalytic activity
C	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005886	cellular_component	plasma membrane
C	0006103	biological_process	2-oxoglutarate metabolic process
C	0006520	biological_process	amino acid metabolic process
C	0006531	biological_process	aspartate metabolic process
C	0006533	biological_process	L-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	0016740	molecular_function	transferase activity
C	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0043490	biological_process	malate-aspartate shuttle
C	0045471	biological_process	response to ethanol
C	0070062	cellular_component	extracellular exosome
D	0003723	molecular_function	RNA binding
D	0003824	molecular_function	catalytic activity
D	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005886	cellular_component	plasma membrane
D	0006103	biological_process	2-oxoglutarate metabolic process
D	0006520	biological_process	amino acid metabolic process
D	0006531	biological_process	aspartate metabolic process
D	0006533	biological_process	L-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	0016740	molecular_function	transferase activity
D	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0043490	biological_process	malate-aspartate shuttle
D	0045471	biological_process	response to ethanol
D	0070062	cellular_component	extracellular exosome

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	16
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	44
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine; alternate","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P12344","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Asymmetric dimethylarginine","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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