| Link type | Probability | Loop ranges | Chain A piercings | Chain C piercings | Chain F piercings | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
|
Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
| view details |
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Hopf.2 U Ring | 32% | -A | -250A -268F | ||||||||||
Chain A Sequence |
RPSTPTILGYEVMEERAKFTVYKILVKKTPEESWVVFRRYTDFSRLNDKLKEMFPGFRLALPPKRWFKDNYNADFLEDRQLGLQAFLQNLVAHKDIANCLAVREFLCLDDPPGPFDSLEESRAFCETLEETNYRLQKELLEKQKEMESLKKLLSEKQLHIDTLENRIRTLSLE |
Chain A Sequence |
RPSTPTILGYEVMEERAKFTVYKILVKKTPEESWVVFRRYTDFSRLNDKLKEMFPGFRLALPPKRWFKDNYNADFLEDRQLGLQAFLQNLVAHKDIANCLAVREFLCLDDPPGPFDSLEESRAFCETLEETNYRLQKELLEKQKEMESLKKLLSEKQLHIDTLENRIRTLSLE |
Chain A Sequence |
TPTILGYEVMEERAKFTVYKILVKKTPEE-WVVFRRYTDFSRLNDKLKEMFPGFRLALPPKR-FKDNYNADFLEDRQLGLQAFLQNLVAHKDIANCLAVREFLCLDDPPGPFDSLEESRAFCETLEETNYRLQKELLEKQKEMESLKKLLSEKQLHIDTLENRIRTLSLE |
| sequence length | 173,173,170 |
| structure length | 173,173,168 |
| publication title |
SNX16 Regulates the Recycling of E-Cadherin through a Unique Mechanism of Coordinated Membrane and Cargo Binding.
pubmed doi rcsb |
| molecule tags | Protein transport |
| molecule keywords | Sorting nexin-16 |
| source organism | Homo sapiens |
| missing residues | F: 137-139,170-172 |
| pdb deposition date | 2016-09-08 |
| LinkProt deposition date | 2017-09-16 |
Image from the rcsb pdb (www.rcsb.org)#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...
