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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
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Unlink | 53% | -142A +155A | |||||||||
Chain A Sequence |
SSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK |
Chain A Sequence |
SSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK |
| sequence length | 401,401 |
| structure length | 401,401 |
| publication title |
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains.
pubmed doi rcsb |
| molecule tags | Transferase |
| molecule keywords | Aspartate aminotransferase, mitochondrial |
| source organism | Mus musculus |
| ec nomenclature |
ec 2.6.1.1: Aspartate transaminase. ec 2.6.1.7: Kynurenine--oxoglutarate transaminase. ec 2.6.1.1: Aspartate transaminase. ec 2.6.1.7: Kynurenine--oxoglutarate transaminase. |
| pdb deposition date | 2009-05-27 |
| LinkProt deposition date | 2016-08-17 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| AB | PF00155 | Aminotran_1_2 | Aminotransferase class I and II |
| AB | PF00155 | Aminotran_1_2 | Aminotransferase class I and II |
Image from the rcsb pdb (www.rcsb.org)cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | 3-Layer(aba) Sandwich | Aspartate Aminotransferase; domain 2 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) | ||
| Alpha Beta | Alpha-Beta Complex | Aspartate Aminotransferase, domain 1 | Aspartate Aminotransferase, domain 1 | ||
| Alpha Beta | 3-Layer(aba) Sandwich | Aspartate Aminotransferase; domain 2 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) | ||
| Alpha Beta | Alpha-Beta Complex | Aspartate Aminotransferase, domain 1 | Aspartate Aminotransferase, domain 1 |
#chains in the LinkProt database with same CATH superfamily 3FSL ACD; 1AKA AB; 3FSL CDE; 1ASM AB; 1AIA AB; 1AHX AB; 1AIB AB; 1ARI AB; 3FSL BCD; 3FSL ABD; 3HLM ACD; 3FSL AB; 3FSL BEF; 3FSL CDF; 1AJR AB; 1ARH AB; 1AHG AB; 1ASN AB; 1AHY AB; 3FSL EF; 3FSL DEF; 1AIC AB; 3FSL CEF; 3FSL AEF; 1AHF AB; 3FSL ABF; 3FSL CD; 3HLM CD; 1AHE AB; 1ASL AB; 3HLM AB; 3HLM ABC; 1ARG AB; 3FSL ABC; 3FSL ABE; #chains in the LinkProt database with same CATH topology 3FSL ACD; 1AKA AB; 3FSL CDE; 1ASM AB; 1AIA AB; 1AHX AB; 1AIB AB; 1ARI AB; 3FSL BCD; 3FSL ABD; 3HLM ACD; 3FSL AB; 3FSL BEF; 3FSL CDF; 1AJR AB; 1ARH AB; 1AHG AB; 1ASN AB; 1AHY AB; 3FSL EF; 3FSL DEF; 1AIC AB; 3FSL CEF; 3FSL AEF; 1AHF AB; 3FSL ABF; 3FSL CD; 3HLM CD; 1AHE AB; 1ASL AB; 3HLM AB; 3HLM ABC; 1ARG AB; 3FSL ABC; 3FSL ABE; #chains in the LinkProt database with same CATH homology 3FSL ACD; 1AKA AB; 3FSL CDE; 1ASM AB; 1AIA AB; 1AHX AB; 1AIB AB; 1ARI AB; 3FSL BCD; 3FSL ABD; 3HLM ACD; 3FSL AB; 3FSL BEF; 3FSL CDF; 1AJR AB; 1ARH AB; 1AHG AB; 1ASN AB; 1AHY AB; 3FSL EF; 3FSL DEF; 1AIC AB; 3FSL CEF; 3FSL AEF; 1AHF AB; 3FSL ABF; 3FSL CD; 3HLM CD; 1AHE AB; 1ASL AB; 3HLM AB; 3HLM ABC; 1ARG AB; 3FSL ABC; 3FSL ABE;
#similar chains in the LinkProt database (?% sequence similarity) ...loading similar chains, please wait... #similar chains, but unlinked ...loading similar chains, please wait... #similar chains in the pdb database (?% sequence similarity) ...loading similar chains, please wait...
