PCNA complex with Cdt2 C-terminal PIP-box peptide. Determined by X-ray diffraction at 3.5 Å resolution. Released 23 Jan 2019.
Explore 6QC0 in 3D Show helices and sheets RCSB PDB PDBe
6QC0 contains 20 α-helices and 59 β-strands across 4 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 | 2-6 | 5 | 1 |
| α-helix | 9-20 | 12 | |
| β-strand | 25-31 | 7 | 2 |
| β-strand | 34-40 | 7 | 2 |
| β-strand | 46-53 | 8 | 2 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-61 | 3 | 1 |
| β-strand | 66-71 | 6 | 2 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 1 |
| β-strand | 98-104 | 7 | 1 |
| β-strand | 110-117 | 8 | 1 |
| β-strand | 119 | 1 | 2 |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-162 | 6 | 3 |
| β-strand | 166-172 | 7 | 3 |
| β-strand | 176-183 | 8 | 3 |
| β-strand | 196-199 | 4 | 2 |
| β-strand | 203-208 | 6 | 3 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-230 | 7 | 2 |
| β-strand | 233-241 | 9 | 2 |
| β-strand | 245-251 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 4 |
| α-helix | 9-20 | 12 | |
| β-strand | 25-31 | 7 | 5 |
| β-strand | 34-40 | 7 | 5 |
| β-strand | 46-53 | 8 | 5 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 4 |
| β-strand | 66-71 | 6 | 5 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 4 |
| β-strand | 98-104 | 7 | 4 |
| α-helix | 105 | 1 | |
| β-strand | 110-117 | 8 | 4 |
| β-strand | 119 | 1 | 5 |
| β-strand | 135-140 | 6 | 5 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-162 | 6 | 1 |
| β-strand | 166-172 | 7 | 1 |
| β-strand | 176-183 | 8 | 1 |
| β-strand | 196-199 | 4 | 5 |
| β-strand | 203-208 | 6 | 1 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-230 | 7 | 5 |
| β-strand | 233-241 | 9 | 5 |
| β-strand | 245-251 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 3 |
| α-helix | 9-20 | 12 | |
| β-strand | 25-31 | 7 | 6 |
| β-strand | 34-40 | 7 | 6 |
| β-strand | 46-53 | 8 | 6 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 3 |
| β-strand | 66-71 | 6 | 6 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 3 |
| β-strand | 98-104 | 7 | 3 |
| β-strand | 110-117 | 8 | 3 |
| β-strand | 119 | 1 | 6 |
| β-strand | 135-140 | 6 | 6 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-162 | 6 | 4 |
| β-strand | 166-172 | 7 | 4 |
| β-strand | 176-183 | 8 | 4 |
| β-strand | 196-199 | 4 | 6 |
| β-strand | 203-208 | 6 | 4 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-230 | 7 | 6 |
| β-strand | 233-241 | 9 | 6 |
| β-strand | 245-251 | 7 | 6 |
| β-strand | 254 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 706 | 1 | 7 |
| α-helix | 709-712 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proliferating cell nuclear antigen | A, C, E | protein | 263 | Homo sapiens | P12004 (AlphaFold model) |
| Denticleless protein homolog | B, D, F | protein | 14 | Homo sapiens | Q9NZJ0 (AlphaFold model) |
>6QC0_1 Proliferating cell nuclear antigen (chains A, C, E) GPMFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFD TYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKL MDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNG NIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVE YKIADMGHLKYYLAPKIEDEEGS
>6QC0_2 Denticleless protein homolog (chains B, D, F) SSMRKICTYFHRKS
Direct binding of Cdt2 to PCNA is important for targeting the CRL4Cdt2E3 ligase activity to Cdt1. Hayashi, A., Giakoumakis, N.N., Heidebrecht, T. et al. Life Sci Alliance (2018) 1:e201800238-e201800238. DOI 10.26508/lsa.201800238 · PubMed
Other PDB entries of the same protein (UniProt P12004 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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