Crystal structure of insulin degrading enzyme complexed with inhibitor. Determined by X-ray diffraction at 2.21 Å resolution. Released 17 Jun 2015.
Explore 4PFC in 3D Show helices and sheets RCSB PDB PDBe
4PFC contains 112 α-helices and 68 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 |
|---|---|---|---|
| β-strand | 47-50 | 4 | 1 |
| β-strand | 63-69 | 7 | 1 |
| β-strand | 74-79 | 6 | 1 |
| β-strand | 85-92 | 8 | 1 |
| α-helix | 96-98 | 3 | |
| α-helix | 106-114 | 9 | |
| β-strand | 118 | 1 | 2 |
| α-helix | 126-133 | 8 | |
| β-strand | 137-142 | 6 | 1 |
| β-strand | 147-154 | 8 | 1 |
| α-helix | 155-157 | 3 | |
| α-helix | 158-166 | 9 | |
| α-helix | 167-169 | 3 | |
| β-strand | 172 | 1 | 2 |
| α-helix | 176-178 | 3 | |
| α-helix | 179-194 | 16 | |
| α-helix | 197-207 | 11 | |
| α-helix | 214-216 | 3 | |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-232 | 4 | |
| α-helix | 237-248 | 12 | |
| α-helix | 251-253 | 3 | |
| β-strand | 254-260 | 7 | 1 |
| α-helix | 264-275 | 12 | |
| α-helix | 283-286 | 4 | |
| α-helix | 295-297 | 3 | |
| β-strand | 300-304 | 5 | 3 |
| β-strand | 312-320 | 9 | 3 |
| α-helix | 323-325 | 3 | |
| α-helix | 330-338 | 9 | |
| α-helix | 346-352 | 7 | |
| β-strand | 359-367 | 9 | 3 |
| β-strand | 370-378 | 9 | 3 |
| α-helix | 383-385 | 3 | |
| α-helix | 387-404 | 18 | |
| α-helix | 408-423 | 16 | |
| α-helix | 425-429 | 5 | |
| α-helix | 430-440 | 11 | |
| α-helix | 446-448 | 3 | |
| α-helix | 461-468 | 8 | |
| α-helix | 473-475 | 3 | |
| β-strand | 477-481 | 5 | 3 |
| α-helix | 483-485 | 3 | |
| β-strand | 491-493 | 3 | 3 |
| β-strand | 498-504 | 7 | 3 |
| α-helix | 505-506 | 2 | |
| α-helix | 507-514 | 8 | |
| α-helix | 538-541 | 4 | |
| β-strand | 549-553 | 5 | 4 |
| β-strand | 557-563 | 7 | 4 |
| β-strand | 571-579 | 9 | 4 |
| α-helix | 587-613 | 27 | |
| β-strand | 616-622 | 7 | 4 |
| β-strand | 626-634 | 9 | 4 |
| α-helix | 638-650 | 13 | |
| α-helix | 656-671 | 16 | |
| α-helix | 672-675 | 4 | |
| α-helix | 678-690 | 13 | |
| β-strand | 691 | 1 | 5 |
| α-helix | 697-704 | 8 | |
| α-helix | 709-721 | 13 | |
| β-strand | 722-723 | 2 | 6 |
| β-strand | 724-731 | 8 | 4 |
| α-helix | 735-753 | 19 | |
| β-strand | 756-757 | 2 | 6 |
| α-helix | 758-759 | 2 | |
| α-helix | 760-762 | 3 | |
| α-helix | 766-767 | 2 | |
| β-strand | 768 | 1 | 5 |
| β-strand | 769 | 1 | 7 |
| α-helix | 771-772 | 2 | |
| β-strand | 775-782 | 8 | 8 |
| β-strand | 789-799 | 11 | 8 |
| α-helix | 802-819 | 18 | |
| α-helix | 820-826 | 7 | |
| β-strand | 830-840 | 11 | 8 |
| β-strand | 843-852 | 10 | 8 |
| α-helix | 856-876 | 21 | |
| α-helix | 879-894 | 16 | |
| α-helix | 900-912 | 13 | |
| α-helix | 920-930 | 11 | |
| α-helix | 933-943 | 11 | |
| β-strand | 952-959 | 8 | 8 |
| β-strand | 990-991 | 2 | 8 |
| α-helix | 995-1000 | 6 | |
| β-strand | 1004 | 1 | 7 |
| α-helix | 1008-1010 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 47-50 | 4 | 9 |
| β-strand | 63-69 | 7 | 9 |
| β-strand | 74-79 | 6 | 9 |
| β-strand | 85-92 | 8 | 9 |
| α-helix | 96-98 | 3 | |
| α-helix | 106-114 | 9 | |
| β-strand | 118 | 1 | 10 |
| α-helix | 125-133 | 9 | |
| β-strand | 137-142 | 6 | 9 |
| β-strand | 147-154 | 8 | 9 |
| α-helix | 155-157 | 3 | |
| α-helix | 158-167 | 10 | |
| β-strand | 172 | 1 | 10 |
| α-helix | 176-178 | 3 | |
| α-helix | 179-193 | 15 | |
| α-helix | 197-207 | 11 | |
| α-helix | 214-216 | 3 | |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-232 | 4 | |
| α-helix | 237-248 | 12 | |
| α-helix | 251-253 | 3 | |
| β-strand | 254-260 | 7 | 9 |
| α-helix | 264-275 | 12 | |
| α-helix | 279-280 | 2 | |
| α-helix | 283-286 | 4 | |
| α-helix | 295-297 | 3 | |
| β-strand | 300-304 | 5 | 11 |
| β-strand | 312-319 | 8 | 11 |
| α-helix | 323-325 | 3 | |
| α-helix | 330-338 | 9 | |
| α-helix | 346-352 | 7 | |
| β-strand | 359-367 | 9 | 11 |
| β-strand | 370-378 | 9 | 11 |
| α-helix | 383-385 | 3 | |
| α-helix | 387-404 | 18 | |
| α-helix | 408-423 | 16 | |
| α-helix | 425-429 | 5 | |
| α-helix | 430-440 | 11 | |
| α-helix | 446-448 | 3 | |
| α-helix | 461-468 | 8 | |
| α-helix | 473-475 | 3 | |
| β-strand | 477-481 | 5 | 11 |
| α-helix | 483-485 | 3 | |
| β-strand | 491-492 | 2 | 11 |
| β-strand | 499-504 | 6 | 11 |
| α-helix | 505-506 | 2 | |
| α-helix | 507-514 | 8 | |
| α-helix | 536-541 | 6 | |
| β-strand | 549-553 | 5 | 12 |
| β-strand | 557-563 | 7 | 12 |
| β-strand | 571-579 | 9 | 12 |
| α-helix | 587-613 | 27 | |
| β-strand | 616-622 | 7 | 12 |
| β-strand | 626-634 | 9 | 12 |
| α-helix | 638-651 | 14 | |
| α-helix | 656-671 | 16 | |
| α-helix | 672-675 | 4 | |
| α-helix | 678-690 | 13 | |
| β-strand | 691 | 1 | 13 |
| α-helix | 697-704 | 8 | |
| α-helix | 709-720 | 12 | |
| β-strand | 722-723 | 2 | 14 |
| β-strand | 724-731 | 8 | 12 |
| α-helix | 735-753 | 19 | |
| β-strand | 756-757 | 2 | 14 |
| α-helix | 758-759 | 2 | |
| α-helix | 760-762 | 3 | |
| α-helix | 766-767 | 2 | |
| β-strand | 768 | 1 | 13 |
| β-strand | 769 | 1 | 7 |
| α-helix | 771-772 | 2 | |
| β-strand | 775-782 | 8 | 15 |
| β-strand | 789-799 | 11 | 15 |
| α-helix | 802-819 | 18 | |
| α-helix | 820-826 | 7 | |
| β-strand | 832-840 | 9 | 15 |
| β-strand | 843-852 | 10 | 15 |
| α-helix | 856-876 | 21 | |
| α-helix | 879-893 | 15 | |
| α-helix | 895-897 | 3 | |
| α-helix | 900-912 | 13 | |
| α-helix | 920-928 | 9 | |
| α-helix | 933-939 | 7 | |
| α-helix | 940-944 | 5 | |
| β-strand | 952-959 | 8 | 15 |
| α-helix | 981-984 | 4 | |
| α-helix | 986-989 | 4 | |
| β-strand | 990-991 | 2 | 15 |
| α-helix | 995-1000 | 6 | |
| β-strand | 1004 | 1 | 7 |
| α-helix | 1007-1011 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Insulin-degrading enzyme | A, B | protein | 989 | Homo sapiens | P14735 (AlphaFold model) |
>4PFC_1 Insulin-degrading enzyme (chains A, B) MGHHHHHHGRAMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAAL DVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYY FDVSHEHLEGALDRFAQFFLSPLFDESAKDREVNAVDSEHEKNVMNDAWRLFQLEKATGN PKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVVVLGRESLDDLTNL VVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNP GHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDI ILHMFQYIQKLRAEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVL TAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVI KKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLP KANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLS VKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLM TEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLI EHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSENMFLEL FAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITM EKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKT LTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSNPVVGEFPAQNDINLSQAPALPQPE VIQNMTEFKRGLPLFPLVKPHINFMAAKL
| ID | Name | Formula | Copies |
|---|---|---|---|
| 2QX | methyl [(2S)-2-(5-{5-[4-({(2S)-2-[(3S)-3-amino-2-oxopiperidin-1-yl]-2-cyclohexy… | C44 H54 F N5 O4 | 2 |
| ZN | Zinc ion | Zn | 2 |
Dual Exosite-binding Inhibitors of Insulin-degrading Enzyme Challenge Its Role as the Primary Mediator of Insulin Clearance in Vivo. Durham, T.B., Toth, J.L., Klimkowski, V.J. et al. J Biol Chem (2015) 290:20044-20059. DOI 10.1074/jbc.M115.638205 · PubMed
Other PDB entries of the same protein (UniProt P14735 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4PFC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.