DNA polymerase IV - DNA ternary complex 12. Determined by X-ray diffraction at 2.09 Å resolution. Released 14 Nov 2018.
Explore 5YV0 in 3D Show helices and sheets RCSB PDB PDBe
5YV0 contains 37 α-helices and 36 β-strands across 2 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 | 4-9 | 6 | 7 |
| α-helix | 12-20 | 9 | |
| α-helix | 22-24 | 3 | |
| β-strand | 29-32 | 4 | 8 |
| β-strand | 40 | 1 | 9 |
| β-strand | 41-44 | 4 | 8 |
| α-helix | 46-49 | 4 | |
| β-strand | 58 | 1 | 9 |
| α-helix | 59-65 | 7 | |
| β-strand | 70-72 | 3 | 8 |
| α-helix | 76-93 | 18 | |
| β-strand | 97-101 | 5 | 7 |
| β-strand | 104-108 | 5 | 7 |
| α-helix | 115-117 | 3 | |
| α-helix | 119-134 | 16 | |
| β-strand | 138-143 | 6 | 7 |
| α-helix | 146-153 | 8 | |
| β-strand | 161-163 | 3 | 7 |
| α-helix | 166-168 | 3 | |
| α-helix | 169-174 | 6 | |
| β-strand | 177 | 1 | 10 |
| α-helix | 178-180 | 3 | |
| α-helix | 186-194 | 9 | |
| β-strand | 199 | 1 | 10 |
| α-helix | 200-204 | 5 | |
| α-helix | 208-213 | 6 | |
| α-helix | 217-225 | 9 | |
| α-helix | 232-234 | 3 | |
| β-strand | 242-253 | 12 | 11 |
| α-helix | 256-277 | 22 | |
| β-strand | 282 | 1 | 12 |
| β-strand | 285-292 | 8 | 11 |
| β-strand | 297-303 | 7 | 11 |
| β-strand | 306 | 1 | 12 |
| α-helix | 309-323 | 15 | |
| β-strand | 329-337 | 9 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 1 |
| α-helix | 12-20 | 9 | |
| α-helix | 22-24 | 3 | |
| β-strand | 29-32 | 4 | 2 |
| β-strand | 40 | 1 | 3 |
| β-strand | 41-44 | 4 | 2 |
| α-helix | 46-49 | 4 | |
| β-strand | 58 | 1 | 3 |
| α-helix | 59-65 | 7 | |
| α-helix | 69 | 1 | |
| β-strand | 70-72 | 3 | 2 |
| α-helix | 76-91 | 16 | |
| β-strand | 97-101 | 5 | 1 |
| β-strand | 104-108 | 5 | 1 |
| α-helix | 114-117 | 4 | |
| α-helix | 119-134 | 16 | |
| β-strand | 138-143 | 6 | 1 |
| α-helix | 146-155 | 10 | |
| β-strand | 161-163 | 3 | 1 |
| α-helix | 169-174 | 6 | |
| β-strand | 177 | 1 | 4 |
| α-helix | 178-180 | 3 | |
| α-helix | 186-194 | 9 | |
| β-strand | 199 | 1 | 4 |
| α-helix | 200-204 | 5 | |
| α-helix | 208-215 | 8 | |
| α-helix | 217-225 | 9 | |
| α-helix | 232-234 | 3 | |
| β-strand | 242-253 | 12 | 5 |
| α-helix | 256-277 | 22 | |
| β-strand | 282 | 1 | 6 |
| β-strand | 285-292 | 8 | 5 |
| β-strand | 297-303 | 7 | 5 |
| β-strand | 306 | 1 | 6 |
| α-helix | 309-323 | 15 | |
| β-strand | 329-337 | 9 | 5 |
| α-helix | 338-339 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA polymerase IV | A, F | protein | 352 | Escherichia coli K-12 | Q47155 (AlphaFold model) |
| DTN1 | B, G | DNA | 18 | Escherichia coli K-12 | |
| DTN2 | C, H | DNA | 19 | Escherichia coli K-12 |
>5YV0_1 DNA polymerase IV (chains A, F) GSRKIIHVDMDCFFAAVEMRDNPALRDIPIAIGGSRERRGVISTANYPARKFGVRSAMPT GMALKLCPHLTLLPGRFDAYKEASNHIREIFSRYTSRIEPLSLDEAYLDVTDSVHCHGSA TLIAQEIRQTIFNELQLTASAGVAPVKFLAKIASDMNKPNGQFVITPAEVPAFLQTLPLA KIPGVGKVSAAKLEAMGLRTCGDVQKCDLVMLLKRFGKFGRILWERSQGIDERDVNSERL RKSVGVERTMAEDIHHWSECEAIIERLYPELERRLAKVKPDLLIARQGVKLKFDDFQQTT QEHVWPRLNKADLIATARKTWDERRGGRGVRLVGLHVTLLDPQMERQLVLGL
>5YV0_2 DTN1 (chains B, G) TCTAGGGTCCTAGGACCC
>5YV0_3 DTN2 (chains C, H) TCTAGGGTCCTAGGACCCT
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 4 |
| PO4 | Phosphate ion | O4 P | 2 |
| DPO | Diphosphate | O7 P2 | 1 |
| TTP | Thymidine-5'-triphosphate | C10 H17 N2 O14 P3 | 1 |
Pyrophosphate hydrolysis is an intrinsic and critical step of the DNA synthesis reaction. Kottur, J., Nair, D.T. Nucleic Acids Res (2018) 46:5875-5885. DOI 10.1093/nar/gky402 · PubMed
Other PDB entries of the same protein (UniProt Q47155 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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