Structure of human DPP3 in complex with endomorphin-2. Determined by X-ray diffraction at 2.38 Å resolution. Released 13 Apr 2016.
Explore 5EHH in 3D Show helices and sheets RCSB PDB PDBe
5EHH contains 39 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 | 131-135 | 5 | |
| α-helix | 137-152 | 16 | |
| α-helix | 156-158 | 3 | |
| 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 |
| β-strand | 236-239 | 4 | 6 |
| β-strand | 242-250 | 9 | 6 |
| α-helix | 252-266 | 15 | |
| 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 | 354-356 | 3 | |
| 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 | 429-448 | 20 | |
| α-helix | 449-455 | 7 | |
| 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 |
| α-helix | 485 | 1 | |
| β-strand | 489 | 1 | 8 |
| α-helix | 495-499 | 5 | |
| α-helix | 500-502 | 3 | |
| α-helix | 503-518 | 16 | |
| α-helix | 522-527 | 6 | |
| α-helix | 533-552 | 20 | |
| α-helix | 553-556 | 4 | |
| β-strand | 557-558 | 2 | 11 |
| β-strand | 563-564 | 2 | 11 |
| α-helix | 567-582 | 16 | |
| β-strand | 587-593 | 7 | 12 |
| β-strand | 599-605 | 7 | 12 |
| α-helix | 607-610 | 4 | |
| α-helix | 614-630 | 17 | |
| α-helix | 634-644 | 11 | |
| α-helix | 655-664 | 10 | |
| α-helix | 668-670 | 3 | |
| β-strand | 671-673 | 3 | 2 |
| β-strand | 676-678 | 3 | 13 |
| β-strand | 685-687 | 3 | 13 |
| α-helix | 693-701 | 9 | |
| α-helix | 708-721 | 14 | |
| α-helix | 723-725 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dipeptidyl peptidase 3 | A | protein | 726 | Homo sapiens | Q9NY33 (AlphaFold model) |
| Endomorphin-2 | B | protein | 5 | Homo sapiens |
>5EHH_1 Dipeptidyl peptidase 3 (chains A) MADTQYILPNDIGVSSLDSREAFRLLSPTERLYAYHLSRAAWYGGLAVLLQTSPEAPYIY ALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPK EKLERVILGSEAAQQHPEEVRGLWQTCGELMFSLEPRLRHLGLGKEGITTYFSGNCTMED AKLAQDFLDSQNLSAYNTRLFKEVDGCGKPYYEVRLASVLGSEPSLDSEVTSKLKSYEFR GSPFQVTRGDYAPILQKVVEQLEKAKAYAANSHQGQMLAQYIESFTQGSIEAHKRGSRFW IQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAVVNKAMSAKFERLVASAEQLLKELPWP PTFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYATQ REKLTFLEEDDKDLYILWKGPSFDVQVGLHALLGHGSGKLFVQDEKGAFNFDQETVINPE TGEQIQSWYRCGETWDSKFSTIASSYEECRAESVGLYLSLHPQVLEIFGFEGADAEDVIY VNWLNMVRAGLLALEFYTPEAFNWRQAHMQARFVILRVLLEAGEGLVTITPTTGSDGRPD ARVRLDRSKIRSVGKPALERFLRRLQVLKSTGDVAGGRALYEGYATVTDAPPESFLTLRD TVLLRKESRKLIVQPNTRLEGSDVQLLEYEASAAGLIRSFSERFPEDGPELEEILTQLAT ADARFW
>5EHH_2 Endomorphin-2 (chains B) YPFFX
Water and common crystallization additives (K) are not listed.
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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