Crystal structure of human PCNA in complex with ZRANB3 APIM motif peptide. Determined by X-ray diffraction at 2.45 Å resolution. Released 28 Jun 2017.
Explore 5MLW in 3D Show helices and sheets RCSB PDB PDBe
5MLW contains 27 α-helices and 65 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 | 10-20 | 11 | |
| 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 | 98-104 | 7 | 1 |
| β-strand | 110-117 | 8 | 1 |
| β-strand | 119 | 1 | 2 |
| β-strand | 127 | 1 | 3 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-162 | 6 | 4 |
| β-strand | 166-173 | 8 | 4 |
| β-strand | 176-183 | 8 | 4 |
| 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 |
| α-helix | 252-254 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1073-1075 | 3 | |
| β-strand | 1077 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 5 |
| α-helix | 10-20 | 11 | |
| β-strand | 25-30 | 6 | 6 |
| β-strand | 34-40 | 7 | 6 |
| β-strand | 46-53 | 8 | 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 | 98-104 | 7 | 5 |
| β-strand | 110-117 | 8 | 5 |
| β-strand | 119 | 1 | 6 |
| β-strand | 127 | 1 | 7 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 6 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-162 | 6 | 1 |
| β-strand | 166-173 | 8 | 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 | 4 |
| α-helix | 10-20 | 11 | |
| β-strand | 25-31 | 7 | 8 |
| β-strand | 34-40 | 7 | 8 |
| β-strand | 46-53 | 8 | 8 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 4 |
| β-strand | 66-71 | 6 | 8 |
| 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 | 8 |
| β-strand | 127 | 1 | 9 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 8 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-162 | 6 | 5 |
| β-strand | 166-173 | 8 | 5 |
| β-strand | 176-183 | 8 | 5 |
| β-strand | 196-199 | 4 | 8 |
| β-strand | 203-208 | 6 | 5 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-229 | 6 | 8 |
| β-strand | 235-241 | 7 | 8 |
| β-strand | 245-251 | 7 | 8 |
| α-helix | 252-253 | 2 | |
| β-strand | 254 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1070 | 1 | 10 |
| α-helix | 1073-1075 | 3 | |
| β-strand | 1077 | 1 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proliferating cell nuclear antigen | A, C, E | protein | 261 | Homo sapiens | P12004 (AlphaFold model) |
| APIM motif peptide | B, D, F | protein | 11 | Homo sapiens | Q5FWF4 (AlphaFold model) |
>5MLW_1 Proliferating cell nuclear antigen (chains A, C, E) MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTY RCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNI KLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK IADMGHLKYYLAPKIEDEEGS
>5MLW_2 APIM motif peptide (chains B, D, F) GSDITRFLVKK
Structural insights into the function of ZRANB3 in replication stress response. Sebesta, M., Cooper, C.D.O., Ariza, A. et al. Nat Commun (2017) 8:15847-15847. DOI 10.1038/ncomms15847 · 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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