Crystal structure of the RNA Polymerase I subcomplex A14/43. Determined by X-ray diffraction at 3.1 Å resolution. Released 15 Jan 2008.
Explore 2RF4 in 3D Show helices and sheets RCSB PDB PDBe
2RF4 contains 24 α-helices and 53 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 |
|---|---|---|---|
| α-helix | 24-27 | 4 | |
| β-strand | 28-29 | 2 | 1 |
| β-strand | 34-35 | 2 | 1 |
| β-strand | 38-48 | 11 | 2 |
| α-helix | 51-53 | 3 | |
| α-helix | 57-69 | 13 | |
| β-strand | 70 | 1 | 2 |
| β-strand | 73-74 | 2 | 2 |
| β-strand | 79-88 | 10 | 2 |
| β-strand | 115-125 | 11 | 2 |
| β-strand | 132-137 | 6 | 3 |
| β-strand | 145-149 | 5 | 3 |
| β-strand | 153-157 | 5 | 3 |
| β-strand | 167 | 1 | 4 |
| β-strand | 218 | 1 | 4 |
| β-strand | 224 | 1 | 4 |
| β-strand | 228-239 | 12 | 3 |
| β-strand | 241-248 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 21-24 | 4 | 2 |
| β-strand | 29-30 | 2 | 2 |
| α-helix | 31-32 | 2 | |
| α-helix | 33-48 | 16 | |
| α-helix | 82-98 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-27 | 2 | |
| β-strand | 28 | 1 | 5 |
| α-helix | 34 | 1 | |
| β-strand | 35 | 1 | 5 |
| α-helix | 36 | 1 | |
| β-strand | 38-47 | 10 | 6 |
| α-helix | 51-53 | 3 | |
| α-helix | 58-61 | 4 | |
| α-helix | 66-69 | 4 | |
| β-strand | 70 | 1 | 6 |
| β-strand | 73-74 | 2 | 6 |
| β-strand | 79-88 | 10 | 6 |
| α-helix | 89-91 | 3 | |
| β-strand | 116-125 | 10 | 6 |
| β-strand | 132-137 | 6 | 7 |
| β-strand | 145-149 | 5 | 7 |
| β-strand | 153-157 | 5 | 7 |
| α-helix | 159-161 | 3 | |
| β-strand | 167 | 1 | 8 |
| β-strand | 218 | 1 | 8 |
| β-strand | 224 | 1 | 8 |
| β-strand | 228-239 | 12 | 7 |
| β-strand | 241-248 | 8 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-27 | 2 | |
| β-strand | 28-29 | 2 | 9 |
| β-strand | 34-35 | 2 | 9 |
| β-strand | 38-47 | 10 | 10 |
| α-helix | 51-53 | 3 | |
| α-helix | 58-69 | 12 | |
| β-strand | 70 | 1 | 10 |
| β-strand | 73-74 | 2 | 10 |
| β-strand | 79-88 | 10 | 10 |
| β-strand | 116-125 | 10 | 10 |
| β-strand | 132-140 | 9 | 11 |
| β-strand | 145-149 | 5 | 11 |
| β-strand | 153-157 | 5 | 11 |
| β-strand | 167 | 1 | 12 |
| β-strand | 170-171 | 2 | 13 |
| β-strand | 211-215 | 5 | 13 |
| β-strand | 218 | 1 | 12 |
| β-strand | 224 | 1 | 12 |
| β-strand | 228-239 | 12 | 11 |
| β-strand | 241-248 | 8 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-20 | 2 | |
| β-strand | 21-24 | 4 | 10 |
| β-strand | 29-30 | 2 | 10 |
| α-helix | 31-32 | 2 | |
| α-helix | 33-48 | 16 | |
| α-helix | 82-98 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA-directed RNA polymerase I subunit RPA4 | A, C, E | protein | 214 | Saccharomyces cerevisiae | P46669 (AlphaFold model) |
| DNA-directed RNA polymerase I subunit RPA4 | B, D, F | protein | 87 | Saccharomyces cerevisiae | P50106 (AlphaFold model) |
>2RF4_1 DNA-directed RNA polymerase I subunit RPA4 (chains A, C, E) MSQVKRANENRETARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYVSLAPMYLENPLQG VMKQHLNPLVMKYNNKVGGVVLGYEGLKILDADPLSKEDTSEKLIKITPDTPFGFTWCHV NLYVWQPQVGDVLEGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVHNDGNRSLGHW VDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTLIS
>2RF4_2 DNA-directed RNA polymerase I subunit RPA4 (chains B, D, F) MMKGSRRTGNNTATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKENIIDIDTNLSSS ISQLKRIQRDFKGLPPAQDFSAAPIQV
Functional architecture of RNA polymerase I. Kuhn, C.D., Geiger, S.R., Baumli, S. et al. Cell (2007) 131:1260-1272. DOI 10.1016/j.cell.2007.10.051 · PubMed
Other PDB entries of the same protein (UniProt P46669 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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