Crystal structure of the human sliding clamp at 2.0 angstrom resolution. Determined by X-ray diffraction at 2.01 Å resolution. Released 26 Aug 2015.
Explore 4RJF in 3D Show helices and sheets RCSB PDB PDBe
4RJF contains 25 α-helices and 67 β-strands across 6 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 | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 1 |
| β-strand | 98-104 | 7 | 1 |
| β-strand | 111-117 | 7 | 1 |
| α-helix | 118 | 1 | |
| β-strand | 121-127 | 7 | 3 |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-162 | 6 | 4 |
| β-strand | 166-173 | 8 | 4 |
| β-strand | 176-183 | 8 | 4 |
| α-helix | 184-185 | 2 | |
| β-strand | 196-199 | 4 | 2 |
| β-strand | 203-208 | 6 | 4 |
| 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 |
| β-strand | 254 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 144 | 1 | 5 |
| α-helix | 147-149 | 3 | |
| β-strand | 152-158 | 7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 6 |
| α-helix | 10-17 | 8 | |
| β-strand | 25-31 | 7 | 7 |
| β-strand | 34-40 | 7 | 7 |
| β-strand | 46-53 | 8 | 7 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 6 |
| β-strand | 66-71 | 6 | 7 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 6 |
| β-strand | 98-104 | 7 | 6 |
| β-strand | 111-117 | 7 | 6 |
| β-strand | 121-127 | 7 | 8 |
| β-strand | 130 | 1 | 3 |
| β-strand | 135-140 | 6 | 7 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-163 | 7 | 9 |
| β-strand | 166-173 | 8 | 9 |
| β-strand | 176-183 | 8 | 9 |
| β-strand | 196-199 | 4 | 7 |
| β-strand | 203-208 | 6 | 9 |
| 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 |
| β-strand | 254 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 11 |
| α-helix | 10-17 | 8 | |
| β-strand | 25-30 | 6 | 12 |
| β-strand | 34-40 | 7 | 12 |
| β-strand | 46-53 | 8 | 12 |
| β-strand | 59-62 | 4 | 11 |
| β-strand | 66-71 | 6 | 12 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 11 |
| β-strand | 98-104 | 7 | 11 |
| β-strand | 111-117 | 7 | 11 |
| β-strand | 122-126 | 5 | 13 |
| β-strand | 135-140 | 6 | 12 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-162 | 6 | 14 |
| β-strand | 166-173 | 8 | 14 |
| β-strand | 176-183 | 8 | 14 |
| α-helix | 184-185 | 2 | |
| β-strand | 196-199 | 4 | 12 |
| β-strand | 203-208 | 6 | 14 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-229 | 6 | 12 |
| β-strand | 235-241 | 7 | 12 |
| β-strand | 245-251 | 7 | 12 |
| α-helix | 252-253 | 2 | |
| β-strand | 254 | 1 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 144 | 1 | 15 |
| α-helix | 145-146 | 2 | |
| α-helix | 147-149 | 3 | |
| β-strand | 153-157 | 5 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proliferating cell nuclear antigen | A, C, E | protein | 261 | Homo sapiens | P12004 (AlphaFold model) |
| Cyclin-dependent kinase inhibitor 1 | B, D, F | protein | 22 | Homo sapiens | P38936 (AlphaFold model) |
>4RJF_1 Proliferating cell nuclear antigen (chains A, C, E) MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTY RCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNI KLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK IADMGHLKYYLAPKIEDEEGS
>4RJF_2 Cyclin-dependent kinase inhibitor 1 (chains B, D, F) GRKRRQTSMTDFFHSKRRLIFS
p21 Exploits Residue Tyr151 as a Tether for High-Affinity PCNA Binding. Kroker, A.J., Bruning, J.B. Biochemistry (2015) 54:3483-3493. DOI 10.1021/acs.biochem.5b00241 · 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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