Native human pcna. Determined by X-ray diffraction at 2.3 Å resolution. Released 13 Jan 2005.
Explore 1VYM in 3D Show helices and sheets RCSB PDB PDBe
1VYM contains 26 α-helices and 57 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 |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| α-helix | 10-17 | 8 | |
| 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 | 59-62 | 4 | 1 |
| β-strand | 66-71 | 6 | 2 |
| α-helix | 72-80 | 9 | |
| β-strand | 87-92 | 6 | 1 |
| β-strand | 99-104 | 6 | 1 |
| β-strand | 110-116 | 7 | 1 |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-163 | 7 | 3 |
| β-strand | 166-173 | 8 | 3 |
| β-strand | 176-183 | 8 | 3 |
| α-helix | 184 | 1 | |
| β-strand | 185 | 1 | 4 |
| β-strand | 195 | 1 | 4 |
| β-strand | 196-199 | 4 | 2 |
| β-strand | 204-208 | 5 | 3 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-229 | 6 | 2 |
| α-helix | 234 | 1 | |
| β-strand | 235-241 | 7 | 2 |
| β-strand | 245-251 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 5 |
| α-helix | 9-17 | 9 | |
| β-strand | 25-31 | 7 | 6 |
| β-strand | 34-40 | 7 | 6 |
| β-strand | 47-53 | 7 | 6 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 5 |
| β-strand | 66-71 | 6 | 6 |
| α-helix | 72-80 | 9 | |
| β-strand | 87-92 | 6 | 5 |
| β-strand | 99-104 | 6 | 5 |
| β-strand | 110-116 | 7 | 5 |
| α-helix | 117-118 | 2 | |
| β-strand | 119 | 1 | 6 |
| β-strand | 135-140 | 6 | 6 |
| 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 | 6 |
| β-strand | 203-208 | 6 | 1 |
| 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 |
| α-helix | 252-254 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 3 |
| α-helix | 10-17 | 8 | |
| β-strand | 25-31 | 7 | 7 |
| β-strand | 34-40 | 7 | 7 |
| β-strand | 47-53 | 7 | 7 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 3 |
| β-strand | 66-71 | 6 | 7 |
| α-helix | 72-79 | 8 | |
| α-helix | 86 | 1 | |
| β-strand | 87-92 | 6 | 3 |
| β-strand | 98-104 | 7 | 3 |
| β-strand | 110-117 | 8 | 3 |
| α-helix | 118 | 1 | |
| α-helix | 122-124 | 3 | |
| β-strand | 135-140 | 6 | 7 |
| α-helix | 141-154 | 14 | |
| β-strand | 157-163 | 7 | 5 |
| β-strand | 166-173 | 8 | 5 |
| β-strand | 176-182 | 7 | 5 |
| α-helix | 183-185 | 3 | |
| β-strand | 196-199 | 4 | 7 |
| β-strand | 203-208 | 6 | 5 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-229 | 6 | 7 |
| β-strand | 235-241 | 7 | 7 |
| β-strand | 245-251 | 7 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proliferating cell nuclear antigen | A, B, C | protein | 261 | HOMO SAPIENS | P12004 (AlphaFold model) |
>1VYM_1 PROLIFERATING CELL NUCLEAR ANTIGEN (chains A, B, C) MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTY RCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNI KLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK IADMGHLKYYLAPKIEDEEGS
Structural and Biochemical Studies of Human Proliferating Cell Nuclear Antigen Complexes Provide a Rationale for Cyclin Association and Inhibitor Design. Kontopidis, G., Wu, S., Zheleva, D. et al. Proc Natl Acad Sci U S A (2005) 102:1871. DOI 10.1073/PNAS.0406540102 · 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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