3HLMACD

Crystal structure of mouse mitochondrial aspartate aminotransferase/kynurenine aminotransferase iv
Link type Probability Chain A piercings Chain C piercings Chain D piercings
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
view details
Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
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Unlink Unlink 44% +37A -431A
Interpreting sequences
Chain A Sequence
SSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK
Chain A Sequence
SSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK
Chain A Sequence
SSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK
sequence length 401,401,401
structure length 401,401,401
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.
ec 2.6.1.1: Aspartate transaminase.
ec 2.6.1.7: Kynurenine--oxoglutarate transaminase.
pdb deposition date2009-05-27
LinkProt deposition date2016-08-17

pfam database annotations

chain Pfam Accession CodePfam Family IdentifierPfam Description
ACD PF00155 Aminotran_1_2Aminotransferase class I and II
ACD PF00155 Aminotran_1_2Aminotransferase class I and II
ACD PF00155 Aminotran_1_2Aminotransferase class I and II
Image from the rcsb pdb (www.rcsb.org)
cath code
ClassArchitectureTopologyHomologyDomain
3.40.640.10 Alpha Beta 3-Layer(aba) Sandwich Aspartate Aminotransferase; domain 2 Type I PLP-dependent aspartate aminotransferase-like (Major domain) 3hlmA02
3.90.1150.10 Alpha Beta Alpha-Beta Complex Aspartate Aminotransferase, domain 1 Aspartate Aminotransferase, domain 1 3hlmA01
3.40.640.10 Alpha Beta 3-Layer(aba) Sandwich Aspartate Aminotransferase; domain 2 Type I PLP-dependent aspartate aminotransferase-like (Major domain) 3hlmC02
3.90.1150.10 Alpha Beta Alpha-Beta Complex Aspartate Aminotransferase, domain 1 Aspartate Aminotransferase, domain 1 3hlmC01
3.40.640.10 Alpha Beta 3-Layer(aba) Sandwich Aspartate Aminotransferase; domain 2 Type I PLP-dependent aspartate aminotransferase-like (Major domain) 3hlmD02
3.90.1150.10 Alpha Beta Alpha-Beta Complex Aspartate Aminotransferase, domain 1 Aspartate Aminotransferase, domain 1 3hlmD01
3FSLACD 1AKAAB 3FSLCDE 1ASMAB 1AIAAB 1AHXAB 1AIBAB 1ARIAB 3FSLBCD 3FSLABD 3HLMACD 3FSLAB 3FSLBEF 3FSLCDF 1AJRAB 1ARHAB 1AHGAB 1ASNAB 1AHYAB 3FSLEF 3FSLDEF 1AICAB 3FSLCEF 3FSLAEF 1AHFAB 3FSLABF 3FSLCD 3HLMCD 1AHEAB 1ASLAB 3HLMAB 3HLMABC 1ARGAB 3FSLABC 3FSLABE
chains in the LinkProt database with same CATH superfamily
3FSLACD 1AKAAB 3FSLCDE 1ASMAB 1AIAAB 1AHXAB 1AIBAB 1ARIAB 3FSLBCD 3FSLABD 3HLMACD 3FSLAB 3FSLBEF 3FSLCDF 1AJRAB 1ARHAB 1AHGAB 1ASNAB 1AHYAB 3FSLEF 3FSLDEF 1AICAB 3FSLCEF 3FSLAEF 1AHFAB 3FSLABF 3FSLCD 3HLMCD 1AHEAB 1ASLAB 3HLMAB 3HLMABC 1ARGAB 3FSLABC 3FSLABE
chains in the LinkProt database with same CATH topology
3FSLACD 1AKAAB 3FSLCDE 1ASMAB 1AIAAB 1AHXAB 1AIBAB 1ARIAB 3FSLBCD 3FSLABD 3HLMACD 3FSLAB 3FSLBEF 3FSLCDF 1AJRAB 1ARHAB 1AHGAB 1ASNAB 1AHYAB 3FSLEF 3FSLDEF 1AICAB 3FSLCEF 3FSLAEF 1AHFAB 3FSLABF 3FSLCD 3HLMCD 1AHEAB 1ASLAB 3HLMAB 3HLMABC 1ARGAB 3FSLABC 3FSLABE
chains in the LinkProt database with same CATH homology


 
#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; 
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#similar chains in the LinkProt database (?% sequence similarity)
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LinkProt | Interdisciplinary Laboratory of Biological Systems Modelling