Crystal structure of human PCNA in complex with p15 peptide. Determined by X-ray diffraction at 2.65 Å resolution. Released 18 Mar 2015.
Explore 4D2G in 3D Show helices and sheets RCSB PDB PDBe
4D2G contains 29 α-helices and 59 β-strands across 5 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 | 1-6 | 6 | 1 |
| α-helix | 10-20 | 11 | |
| β-strand | 25-30 | 6 | 2 |
| β-strand | 34-40 | 7 | 2 |
| β-strand | 46-53 | 8 | 2 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 1 |
| β-strand | 66-71 | 6 | 2 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-93 | 7 | 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 | 141-154 | 14 | |
| 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 | 10-19 | 10 | |
| 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 | 72-80 | 9 | |
| β-strand | 87-92 | 6 | 4 |
| β-strand | 98-104 | 7 | 4 |
| β-strand | 110-117 | 8 | 4 |
| β-strand | 119 | 1 | 5 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 5 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-162 | 6 | 1 |
| β-strand | 166-173 | 8 | 1 |
| β-strand | 176-183 | 8 | 1 |
| α-helix | 184-185 | 2 | |
| 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 |
| α-helix | 252-254 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 3 |
| α-helix | 10-17 | 8 | |
| β-strand | 25-30 | 6 | 6 |
| β-strand | 34-40 | 7 | 6 |
| β-strand | 47-53 | 7 | 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 | 87-93 | 7 | 3 |
| β-strand | 98-104 | 7 | 3 |
| β-strand | 110-117 | 8 | 3 |
| α-helix | 118 | 1 | |
| β-strand | 119 | 1 | 6 |
| α-helix | 126 | 1 | |
| β-strand | 127 | 1 | 7 |
| α-helix | 128-130 | 3 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 52-59 | 8 | |
| α-helix | 62-64 | 3 | |
| α-helix | 65-67 | 3 | |
| β-strand | 70 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 57-59 | 3 | |
| α-helix | 65-67 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proliferating cell nuclear antigen | A, B, C | protein | 264 | HOMO SAPIENS | P12004 (AlphaFold model) |
| P15 | D, E | protein | 21 | SYNTHETIC CONSTRUCT | Q15004 (AlphaFold model) |
>4D2G_1 PROLIFERATING CELL NUCLEAR ANTIGEN (chains A, B, C) GPHMFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGF DTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMK LMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGN GNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVV EYKIADMGHLKYYLAPKIEDEEGS
>4D2G_2 P15 (chains D, E) APVCVRPTPKWQKGIGEFFAA
Structure of P15(Paf)-PCNA Complex and Implications for Clamp Sliding During DNA Replication and Repair. De Biasio, A., De Opakua, A.I., Mortuza, G.B. et al. Nat Commun (2015) 6:6439. DOI 10.1038/NCOMMS7439 · 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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