Crystal structure of PCNA in complex with DNA polymerase iota fragment. Determined by X-ray diffraction at 2.3 Å resolution. Released 10 Feb 2009.
Explore 2ZVM in 3D Show helices and sheets RCSB PDB PDBe
2ZVM contains 32 α-helices and 59 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 | 110-117 | 8 | 1 |
| β-strand | 119 | 1 | 2 |
| α-helix | 123-125 | 3 | |
| β-strand | 127 | 1 | 3 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-163 | 7 | 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 |
| α-helix | 252-254 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 5 |
| α-helix | 10-19 | 10 | |
| 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 | 59-62 | 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 |
| α-helix | 126-129 | 4 | |
| 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 | 4 |
| 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 | 4 |
| β-strand | 66-71 | 6 | 7 |
| α-helix | 72-79 | 8 | |
| 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 | 7 |
| α-helix | 126-130 | 5 | |
| β-strand | 135-140 | 6 | 7 |
| α-helix | 141-154 | 14 | |
| β-strand | 157-162 | 6 | 5 |
| β-strand | 166-173 | 8 | 5 |
| β-strand | 176-183 | 8 | 5 |
| α-helix | 184 | 1 | |
| 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 |
| α-helix | 252-254 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 424-426 | 3 | |
| β-strand | 429 | 1 | 3 |
| α-helix | 431 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 424-427 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proliferating cell nuclear antigen | A, B, C | protein | 261 | Homo sapiens | P12004 (AlphaFold model) |
| DNA polymerase iota | U, V, W | protein | 23 |
>2ZVM_1 Proliferating cell nuclear antigen (chains A, B, C) MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTY RCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNI KLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK IADMGHLKYYLAPKIEDEEGS
>2ZVM_2 DNA polymerase iota (chains U, V, W) ALNTAKKGLIDYYLMPSLSTTSR
Structural Basis for Novel Interactions between Human Translesion Synthesis Polymerases and Proliferating Cell Nuclear Antigen. Hishiki, A., Hashimoto, H., Hanafusa, T. et al. J Biol Chem (2009) 284:10552-10560. DOI 10.1074/jbc.M809745200 · 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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