| Link type | Probability | Chain A piercings | Chain C piercings | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| view details |
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Hopf.1 | 86% | +54C | +58A -83A +243A | ||||||||
| view details |
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Hopf.1 | 86% | +54C | +58A -83A +243A | ||||||||
| view details |
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Hopf.1 | 86% | +54C | +58A -83A +243A | ||||||||
| view details |
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Hopf.1 | 86% | +54C | +58A -83A +243A | ||||||||
Chain A Sequence |
MLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ |
Chain A Sequence |
MLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ |
| sequence length | 201,201 |
| structure length | 201,201 |
| publication title |
Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.
pubmed doi rcsb |
| molecule tags | Lipid transport |
| molecule keywords | APOLIPOPROTEIN A-I |
| source organism | Homo sapiens |
| pdb deposition date | 1997-09-23 |
| LinkProt deposition date | 2016-08-17 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| AC | PF01442 | Apolipoprotein | Apolipoprotein A1/A4/E domain |
| AC | PF01442 | Apolipoprotein | Apolipoprotein A1/A4/E domain |
Image from the rcsb pdb (www.rcsb.org)cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Mainly Alpha | Up-down Bundle | Single alpha-helices involved in coiled-coils or other helix-helix interfaces | Apolipoprotein A-I |
#chains in the LinkProt database with same CATH superfamily 1AV1 CD; 1AV1 ABCD; 1AV1 ACD; 1AV1 AC; 1AV1 BCD; 1AV1 ABC; 1AV1 BC; #chains in the LinkProt database with same CATH topology 1OW6 BD; 1MV8 BCD; 1OW6 ABF; 1MUU ABCD; 1MV8 CD; 1OW6 BF; 1MUU AC; 1OW6 BCF; 3EFF KMN; 1MUU AB; 1MUU BD; 1MV8 BD; 3EFF AN; 1MUU BCD; 1OW6 AB; 3EFF LMN; 1OW6 ABC; 1OW6 ABCF; 1AV1 CD; 1OW6 BDF; 1OW6 AD; 1MV8 AB; 1AV1 BCD; 1AV1 ABC; 3EFF BN; 3EFF CL; 3EFF DK; 1MV8 AC; 3EFF KN; 1AQ5 BC; 3EFF AM; 1AQ5 AB; 1AV1 ABCD; 2P1J AB; 3EFF DL; 1AV1 AC; 3EFF CK; 1MFZ CD; 1OW6 BC; 1MUU CD; 1MUU ABD; 1QEX AB; 1MV8 ABC; 1OW6 BCD; 1AQ5 AC; 1MV8 ABD; 1MFZ AB; 1MUU ACD; 1OW6 ABDF; 1AV1 BC; 1MV8 ACD; 1MUU ABC; 3EFF MN; 1OW6 CF; 3EFF AK; 1OW6 ABD; 1AQ5 ABC; 3EFF BM; 3EFF KL; 1AV1 ACD; 1OW6 ABCD; 1OW6 BCDF; 1MV8 ABCD; #chains in the LinkProt database with same CATH homology 1AV1 CD; 1AV1 ABCD; 1AV1 ACD; 1AV1 AC; 1AV1 BCD; 1AV1 ABC; 1AV1 BC;
