Structure of human DPPIII in complex with the opioid peptide Tynorphin, at 3.0 Angstroms. Determined by X-ray diffraction at 2.98 Å resolution. Released 4 Apr 2012.
Explore 3T6J in 3D Show helices and sheets RCSB PDB PDBe
3T6J contains 40 α-helices and 29 β-strands across 2 chains. 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 |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| β-strand | 14-16 | 3 | 1 |
| α-helix | 21-25 | 5 | |
| α-helix | 28-44 | 17 | |
| α-helix | 47-52 | 6 | |
| α-helix | 56-69 | 14 | |
| α-helix | 72-81 | 10 | |
| α-helix | 86-101 | 16 | |
| β-strand | 106 | 1 | 2 |
| β-strand | 112 | 1 | 3 |
| β-strand | 113 | 1 | 2 |
| α-helix | 120-128 | 9 | |
| α-helix | 131-133 | 3 | |
| α-helix | 137-144 | 8 | |
| α-helix | 148-152 | 5 | |
| α-helix | 156-158 | 3 | |
| β-strand | 160 | 1 | 3 |
| β-strand | 172 | 1 | 4 |
| α-helix | 178-190 | 13 | |
| β-strand | 198-204 | 7 | 4 |
| β-strand | 210-216 | 7 | 4 |
| α-helix | 229-233 | 5 | |
| β-strand | 236-239 | 4 | 4 |
| β-strand | 242-247 | 6 | 4 |
| α-helix | 252-266 | 15 | |
| α-helix | 272-287 | 16 | |
| α-helix | 290-302 | 13 | |
| β-strand | 308-316 | 9 | 5 |
| α-helix | 326 | 1 | |
| β-strand | 327-336 | 10 | 5 |
| α-helix | 341-348 | 8 | |
| α-helix | 350-353 | 4 | |
| α-helix | 354-356 | 3 | |
| α-helix | 361-363 | 3 | |
| β-strand | 373-382 | 10 | 5 |
| β-strand | 389-392 | 4 | 5 |
| α-helix | 396-401 | 6 | |
| β-strand | 405-409 | 5 | 5 |
| α-helix | 410-413 | 4 | |
| α-helix | 432-449 | 18 | |
| α-helix | 450-454 | 5 | |
| α-helix | 455 | 1 | |
| β-strand | 462 | 1 | 6 |
| β-strand | 477 | 1 | 7 |
| β-strand | 484 | 1 | 7 |
| β-strand | 489 | 1 | 6 |
| α-helix | 495-499 | 5 | |
| α-helix | 503-519 | 17 | |
| α-helix | 522-527 | 6 | |
| α-helix | 535-552 | 18 | |
| α-helix | 553-556 | 4 | |
| β-strand | 557-558 | 2 | 8 |
| β-strand | 563-564 | 2 | 8 |
| α-helix | 567-582 | 16 | |
| β-strand | 587-590 | 4 | 9 |
| β-strand | 593 | 1 | 10 |
| β-strand | 599 | 1 | 10 |
| β-strand | 602-605 | 4 | 9 |
| α-helix | 610-614 | 5 | |
| α-helix | 615-630 | 16 | |
| α-helix | 634-644 | 11 | |
| α-helix | 655-664 | 10 | |
| β-strand | 671-673 | 3 | 1 |
| β-strand | 676-679 | 4 | 11 |
| β-strand | 684-687 | 4 | 11 |
| α-helix | 693-701 | 9 | |
| α-helix | 708-722 | 15 | |
| α-helix | 723-725 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dipeptidyl peptidase 3 | A | protein | 726 | Homo sapiens | Q9NY33 (AlphaFold model) |
| Tynorphin | B | protein | 5 | Homo sapiens |
>3T6J_1 Dipeptidyl peptidase 3 (chains A) MADTQYILPNDIGVSSLDCREAFRLLSPTERLYAYHLSRAAWYGGLAVLLQTSPEAPYIY ALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPK EKLERVILGSEAAQQHPEEVRGLWQTCGELMFSLEPRLRHLGLGKEGITTYFSGNCTMED AKLAQDFLDSQNLSAYNTRLFKEVDGEGKPYYEVRLASVLGSEPSLDSEVTSKLKSYEFR GSPFQVTRGDYAPILQKVVEQLEKAKAYAANSHQGQMLAQYIESFTQGSIEAHKRGSRFW IQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAVVNKAMSAKFERLVASAEQLLKELPWP PTFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYATQ REKLTFLEEDDKDLYILWKGPSFDVQVGLHALLGHGSGKLFVQDEKGAFNFDQETVINPE TGEQIQSWYRSGETWDSKFSTIASSYEECRAESVGLYLCLHPQVLEIFGFEGADAEDVIY VNWLNMVRAGLLALEFYTPEAFNWRQAHMQARFVILRVLLEAGEGLVTITPTTGSDGRPD ARVRLDRSKIRSVGKPALERFLRRLQVLKSTGDVAGGRALYEGYATVTDAPPECFLTLRD TVLLRKESRKLIVQPNTRLEGSDVQLLEYEASAAGLIRSFSERFPEDGPELEEILTQLAT ADARFW
>3T6J_2 Tynorphin (chains B) VVYPW
Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III. Bezerra, G.A., Dobrovetsky, E., Viertlmayr, R. et al. Proc Natl Acad Sci U S A (2012) 109:6525-6530. DOI 10.1073/pnas.1118005109 · 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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