Crystal structure of APC3-APC16 complex (Selenomethionine Derivative). Determined by X-ray diffraction at 3.25 Å resolution. Released 24 Dec 2014.
Explore 4RG9 in 3D Show helices and sheets RCSB PDB PDBe
4RG9 contains 68 α-helices and 0 β-strands across 3 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 | 8-17 | 10 | |
| α-helix | 21-34 | 14 | |
| α-helix | 38-50 | 13 | |
| α-helix | 54-63 | 10 | |
| α-helix | 69-81 | 13 | |
| α-helix | 85-93 | 9 | |
| α-helix | 99-102 | 4 | |
| α-helix | 103-110 | 8 | |
| α-helix | 111-113 | 3 | |
| α-helix | 114-127 | 14 | |
| α-helix | 131-144 | 14 | |
| α-helix | 149-158 | 10 | |
| α-helix | 164-167 | 4 | |
| α-helix | 463-483 | 21 | |
| α-helix | 487-495 | 9 | |
| α-helix | 499-503 | 5 | |
| α-helix | 505-518 | 14 | |
| α-helix | 521-534 | 14 | |
| α-helix | 542-552 | 11 | |
| α-helix | 555-568 | 14 | |
| α-helix | 573-585 | 13 | |
| α-helix | 589-602 | 14 | |
| α-helix | 607-619 | 13 | |
| α-helix | 623-636 | 14 | |
| α-helix | 641-654 | 14 | |
| α-helix | 657-670 | 14 | |
| α-helix | 674-687 | 14 | |
| α-helix | 699-704 | 6 | |
| α-helix | 709-721 | 13 | |
| α-helix | 725-738 | 14 | |
| α-helix | 743-754 | 12 | |
| α-helix | 760-772 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-17 | 12 | |
| α-helix | 21-34 | 14 | |
| α-helix | 38-50 | 13 | |
| α-helix | 54-62 | 9 | |
| α-helix | 69-81 | 13 | |
| α-helix | 85-92 | 8 | |
| α-helix | 100-102 | 3 | |
| α-helix | 103-110 | 8 | |
| α-helix | 111-113 | 3 | |
| α-helix | 114-127 | 14 | |
| α-helix | 131-144 | 14 | |
| α-helix | 150-157 | 8 | |
| α-helix | 164-167 | 4 | |
| α-helix | 463-483 | 21 | |
| α-helix | 487-494 | 8 | |
| α-helix | 499-502 | 4 | |
| α-helix | 505-517 | 13 | |
| α-helix | 521-534 | 14 | |
| α-helix | 543-551 | 9 | |
| α-helix | 555-566 | 12 | |
| α-helix | 573-585 | 13 | |
| α-helix | 589-602 | 14 | |
| α-helix | 607-619 | 13 | |
| α-helix | 623-636 | 14 | |
| α-helix | 641-653 | 13 | |
| α-helix | 657-670 | 14 | |
| α-helix | 674-687 | 14 | |
| α-helix | 700-704 | 5 | |
| α-helix | 709-721 | 13 | |
| α-helix | 725-738 | 14 | |
| α-helix | 743-756 | 14 | |
| α-helix | 759-772 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 75-83 | 9 | |
| α-helix | 85-91 | 7 | |
| α-helix | 93-95 | 3 | |
| α-helix | 99-102 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division cycle protein 27 homolog | A, B | protein | 560 | Homo sapiens | P30260 (AlphaFold model) |
| Anaphase-promoting complex subunit 16 | S | protein | 43 | Homo sapiens | Q96DE5 (AlphaFold model) |
>4RG9_1 Cell division cycle protein 27 homolog (chains A, B) GSMTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAY RLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDIVTEFGDSACFTL SLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKFTSLQNFSN CLPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYNTGWVLCQ IGRAYFELSEYMQAERIFSEVRRIENYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDK NSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACF RNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKK SEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIG KVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQ ESSMTDADDTQLHAAESDEF
>4RG9_2 Anaphase-promoting complex subunit 16 (chains S) MQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSENLYFQ
Structure of an APC3-APC16 Complex: Insights into Assembly of the Anaphase-Promoting Complex/Cyclosome. Yamaguchi, M., Yu, S., Qiao, R. et al. J Mol Biol (2015) 427:1748-1764. DOI 10.1016/j.jmb.2014.11.020 · PubMed
Other PDB entries of the same protein (UniProt P30260 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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