| Link type | Probability | Chain A piercings | Chain D piercings | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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Unlink | 80% | -112D +183D | |||||||||
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Unlink | 80% | -112D +183D | |||||||||
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Unlink | 80% | -112D +183D | |||||||||
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Unlink | 80% | -112D +183D | |||||||||
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Unlink | 80% | -112D +183D | |||||||||
| view details |
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Unlink | 80% | -112D +183D | |||||||||
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Unlink | 80% | -112D +183D | |||||||||
Chain A Sequence |
GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM |
Chain A Sequence |
GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM |
| sequence length | 176,176 |
| structure length | 176,176 |
| publication title |
Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping.
pubmed doi rcsb |
| molecule tags | Lactoylglutathione lyase |
| molecule keywords | LACTOYLGLUTATHIONE LYASE |
| source organism | Homo sapiens |
| ec nomenclature |
ec 4.4.1.5: Lactoylglutathione lyase. ec 4.4.1.5: Lactoylglutathione lyase. |
| pdb deposition date | 1997-02-25 |
| LinkProt deposition date | 2016-10-21 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| AD | PF00903 | Glyoxalase | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily |
| AD | PF00903 | Glyoxalase | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily |
Image from the rcsb pdb (www.rcsb.org)cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | Roll | 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1 | 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1 | ||
| Alpha Beta | Roll | 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1 | 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1 |
#chains in the LinkProt database with same CATH superfamily 1NPB ADEF; 1BH5 ABCD; 1NPB BDEF; 1NPB ADE; 1NPB ACE; 1NPB ACDE; 1NPB ABD; 1NPB CD; 1BH5 BD; 1NPB ACEF; 1NPB BDE; 1BH5 AB; 1BH5 BCD; 1BH5 ABC; 1FRO CD; 1NPB CDE; 1BH5 CD; 1NPB ABEF; 1NPB CDEF; 1NPB ACDF; 1NPB EF; 1FRO ABD; 1NPB BEF; 1NPB ABC; 1BH5 ABD; 1NPB AEF; 1NPB BE; 1FRO BC; 1NPB DEF; 1NPB AB; 1NPB DF; 1NPB AE; 1FRO ACD; 1BH5 ACD; 1FRO AD; 1NPB AC; 1BH5 AD; 1BH5 BC; 1NPB AD; 1NPB ABCD; 1NPB ABDE; 1NPB DE; 1NPB ABCE; 1FRO BD; 1NPB ADF; 1NPB ACD; 1FRO ABCD; 1NPB ABE; 1NPB CDF; 1FRO ABC; 1NPB BCDE; 1NPB ABDF; 1BH5 AC; 1FRO AB; 1FRO BCD; #chains in the LinkProt database with same CATH topology 1NPB ADEF; 1BH5 ABCD; 1NPB BDEF; 1NPB ADE; 1NPB ACE; 1NPB ACDE; 1NPB ABD; 1NPB CD; 1BH5 BD; 1NPB ACEF; 1NPB BDE; 1BH5 AB; 1BH5 BCD; 1BH5 ABC; 1FRO CD; 1NPB CDE; 1BH5 CD; 1NPB ABEF; 1NPB CDEF; 1NPB ACDF; 1NPB EF; 1FRO ABD; 1NPB BEF; 1NPB ABC; 1BH5 ABD; 1NPB AEF; 1NPB BE; 1FRO BC; 1NPB DEF; 1NPB AB; 1NPB DF; 1NPB AE; 1FRO ACD; 1BH5 ACD; 1FRO AD; 1NPB AC; 1BH5 AD; 1BH5 BC; 1NPB AD; 1NPB ABCD; 1NPB ABDE; 1NPB DE; 1NPB ABCE; 1FRO BD; 1NPB ADF; 1NPB ACD; 1FRO ABCD; 1NPB ABE; 1NPB CDF; 1FRO ABC; 1NPB BCDE; 1NPB ABDF; 1BH5 AC; 1FRO AB; 1FRO BCD; #chains in the LinkProt database with same CATH homology 1NPB ADEF; 1BH5 ABCD; 1NPB BDEF; 1NPB ADE; 1NPB ACE; 1NPB ACDE; 1NPB ABD; 1NPB CD; 1BH5 BD; 1NPB ACEF; 1NPB BDE; 1BH5 AB; 1BH5 BCD; 1BH5 ABC; 1FRO CD; 1NPB CDE; 1BH5 CD; 1NPB ABEF; 1NPB CDEF; 1NPB ACDF; 1NPB EF; 1FRO ABD; 1NPB BEF; 1NPB ABC; 1BH5 ABD; 1NPB AEF; 1NPB BE; 1FRO BC; 1NPB DEF; 1NPB AB; 1NPB DF; 1NPB AE; 1FRO ACD; 1BH5 ACD; 1FRO AD; 1NPB AC; 1BH5 AD; 1BH5 BC; 1NPB AD; 1NPB ABCD; 1NPB ABDE; 1NPB DE; 1NPB ABCE; 1FRO BD; 1NPB ADF; 1NPB ACD; 1FRO ABCD; 1NPB ABE; 1NPB CDF; 1FRO ABC; 1NPB BCDE; 1NPB ABDF; 1BH5 AC; 1FRO AB; 1FRO BCD;
#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...
