Structure of ligand free human DPP3 in closed form. Determined by X-ray diffraction at 2.74 Å resolution. Released 13 Apr 2016.
Explore 5EGY in 3D Show helices and sheets RCSB PDB PDBe
5EGY contains 37 α-helices and 32 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7 | 1 | 1 |
| β-strand | 14-16 | 3 | 2 |
| α-helix | 20-24 | 5 | |
| α-helix | 28-45 | 18 | |
| α-helix | 47-50 | 4 | |
| α-helix | 56-69 | 14 | |
| α-helix | 72-81 | 10 | |
| α-helix | 86-102 | 17 | |
| β-strand | 106 | 1 | 3 |
| β-strand | 112 | 1 | 4 |
| β-strand | 113 | 1 | 3 |
| β-strand | 115 | 1 | 1 |
| α-helix | 120-128 | 9 | |
| α-helix | 132-135 | 4 | |
| α-helix | 137-152 | 16 | |
| β-strand | 160 | 1 | 4 |
| β-strand | 161 | 1 | 5 |
| β-strand | 168 | 1 | 5 |
| β-strand | 172 | 1 | 6 |
| α-helix | 178-190 | 13 | |
| β-strand | 198-204 | 7 | 6 |
| β-strand | 210-217 | 8 | 6 |
| α-helix | 231-233 | 3 | |
| β-strand | 236-239 | 4 | 6 |
| β-strand | 242-250 | 9 | 6 |
| α-helix | 252-267 | 16 | |
| α-helix | 272-287 | 16 | |
| α-helix | 290-302 | 13 | |
| β-strand | 308-316 | 9 | 7 |
| α-helix | 326 | 1 | |
| β-strand | 327-335 | 9 | 7 |
| α-helix | 341-348 | 8 | |
| α-helix | 350-353 | 4 | |
| α-helix | 361-363 | 3 | |
| β-strand | 372-382 | 11 | 7 |
| β-strand | 389-392 | 4 | 7 |
| α-helix | 396-399 | 4 | |
| β-strand | 405-409 | 5 | 7 |
| α-helix | 410-416 | 7 | |
| α-helix | 429-449 | 21 | |
| α-helix | 450-455 | 6 | |
| β-strand | 462 | 1 | 8 |
| β-strand | 463 | 1 | 9 |
| β-strand | 469 | 1 | 9 |
| β-strand | 477 | 1 | 10 |
| β-strand | 484 | 1 | 10 |
| β-strand | 489 | 1 | 8 |
| α-helix | 495-499 | 5 | |
| α-helix | 500-502 | 3 | |
| α-helix | 503-518 | 16 | |
| α-helix | 522-528 | 7 | |
| α-helix | 533-552 | 20 | |
| α-helix | 553-556 | 4 | |
| β-strand | 557-558 | 2 | 11 |
| β-strand | 563-564 | 2 | 11 |
| α-helix | 567-581 | 15 | |
| β-strand | 587-593 | 7 | 12 |
| β-strand | 599-605 | 7 | 12 |
| α-helix | 610-614 | 5 | |
| α-helix | 615-630 | 16 | |
| α-helix | 634-644 | 11 | |
| α-helix | 655-664 | 10 | |
| α-helix | 668-670 | 3 | |
| β-strand | 671-673 | 3 | 2 |
| β-strand | 676-680 | 5 | 13 |
| β-strand | 683-687 | 5 | 13 |
| α-helix | 693-701 | 9 | |
| α-helix | 708-721 | 14 | |
| α-helix | 722-725 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dipeptidyl peptidase 3 | A | protein | 726 | Homo sapiens | Q9NY33 (AlphaFold model) |
>5EGY_1 Dipeptidyl peptidase 3 (chains A) MADTQYILPNDIGVSSLDSREAFRLLSPTERLYAYHLSRAAWYGGLAVLLQTSPEAPYIY ALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPK EKLERVILGSEAAQQHPEEVRGLWQTCGELMFSLEPRLRHLGLGKEGITTYFSGNCTMED AKLAQDFLDSQNLSAYNTRLFKEVDGCGKPYYEVRLASVLGSEPSLDSEVTSKLKSYEFR GSPFQVTRGDYAPILQKVVEQLEKAKAYAANSHQGQMLAQYIESFTQGSIEAHKRGSRFW IQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAVVNKAMSAKFERLVASAEQLLKELPWP PTFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYATQ REKLTFLEEDDKDLYILWKGPSFDVQVGLHALLGHGSGKLFVQDEKGAFNFDQETVINPE TGEQIQSWYRCGETWDSKFSTIASSYEECRAESVGLYLSLHPQVLEIFGFEGADAEDVIY VNWLNMVRAGLLALEFYTPEAFNWRQAHMQARFVILRVLLEAGEGLVTITPTTGSDGRPD ARVRLDRSKIRSVGKPALERFLRRLQVLKSTGDVAGGRALYEGYATVTDAPPESFLTLRD TVLLRKESRKLIVQPNTRLEGSDVQLLEYEASAAGLIRSFSERFPEDGPELEEILTQLAT ADARFW
Substrate complexes of human dipeptidyl peptidase III reveal the mechanism of enzyme inhibition. Kumar, P., Reithofer, V., Reisinger, M. et al. Sci Rep (2016) 6:23787-23787. DOI 10.1038/srep23787 · PubMed
Other PDB entries of the same protein (UniProt Q9NY33 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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