Crystal Structure of Human PCNA in complex with a TRAIP peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Dec 2015.
Explore 4ZTD in 3D Show helices and sheets RCSB PDB PDBe
4ZTD contains 26 α-helices and 57 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 | 4-6 | 3 | 1 |
| α-helix | 9-17 | 9 | |
| 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 | 59-60 | 2 | 1 |
| β-strand | 66-71 | 6 | 2 |
| α-helix | 72-79 | 8 | |
| α-helix | 86 | 1 | |
| β-strand | 87-91 | 5 | 1 |
| β-strand | 98-104 | 7 | 1 |
| β-strand | 110-117 | 8 | 1 |
| β-strand | 119 | 1 | 2 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-162 | 6 | 3 |
| β-strand | 166-173 | 8 | 3 |
| β-strand | 176-183 | 8 | 3 |
| α-helix | 184-185 | 2 | |
| β-strand | 196-199 | 4 | 2 |
| β-strand | 203-208 | 6 | 3 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-229 | 6 | 2 |
| β-strand | 235-241 | 7 | 2 |
| β-strand | 245-251 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 4 |
| α-helix | 9-17 | 9 | |
| 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 | 59-61 | 3 | 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 |
| α-helix | 118 | 1 | |
| β-strand | 119 | 1 | 5 |
| β-strand | 135-140 | 6 | 5 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-162 | 6 | 1 |
| β-strand | 166-172 | 7 | 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 | 224-229 | 6 | 5 |
| β-strand | 235-241 | 7 | 5 |
| β-strand | 245-251 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 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 | 59-61 | 3 | 3 |
| β-strand | 66-71 | 6 | 6 |
| α-helix | 72-80 | 9 | |
| β-strand | 87-91 | 5 | 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 | 141-154 | 14 | |
| 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 | 224-229 | 6 | 6 |
| β-strand | 235-241 | 7 | 6 |
| β-strand | 245-251 | 7 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 463-465 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 460-462 | 3 | |
| α-helix | 464-466 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proliferating cell nuclear antigen | A, B, C | protein | 253 | Homo sapiens | P12004 (AlphaFold model) |
| Ala-phe-gln-ala-lys-leu-asp-thr-phe-leu-trp-ser | D, E | protein | 12 | Homo sapiens | Q9BWF2 (AlphaFold model) |
| Ala-gly-ala-gly-ala | F | protein | 5 | Homo sapiens |
>4ZTD_1 Proliferating cell nuclear antigen (chains A, B, C) FEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYR CDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDL DVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIK LSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKI ADMGHLKYYLAPK
>4ZTD_2 ALA-PHE-GLN-ALA-LYS-LEU-ASP-THR-PHE-LEU-TRP-SER (chains D, E) AFQAKLDTFLWS
>4ZTD_3 ALA-GLY-ALA-GLY-ALA (chains F) AGAGA
TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress. Hoffmann, S., Smedegaard, S., Nakamura, K. et al. J Cell Biol (2016) 212:63-75. DOI 10.1083/jcb.201506071 · 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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