Research workbench
Structure of a 12-subunit nuclear exosome complex bound to single- stranded RNA substrates
Analyse Structure of a 12-subunit nuclear exosome complex bound to single- stranded RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5C0W
- Type
- protein + RNA
- Length
- 3,993 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exosome complex component RRP45; Exosome complex component SKI6; Exosome complex…
- EC
- 3.1.13.-, 3.1.26.-
- UniProt
- Q05636, P46948, P25359, P53256, Q12277, P48240, Q08285, P38792, P53859, Q08162, Q12149, P38801
- Ligands
- MG, ZN
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 14 distinct chains · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exosome complex component RRP45 | protein | 298 | 30% helix, 31% strand | Q05636 |
| B | Exosome complex component SKI6 | protein | 244 | 29% helix, 29% strand | P46948 |
| C | Exosome complex component RRP43 | protein | 321 | 27% helix, 30% strand | P25359 |
| D | Exosome complex component RRP46 | protein | 222 | 33% helix, 36% strand | P53256 |
| E | Exosome complex component RRP42 | protein | 266 | 26% helix, 32% strand | Q12277 |
| F | Exosome complex component MTR3 | protein | 213 | 31% helix, 34% strand | P48240 |
| G | Exosome complex component RRP40 | protein | 236 | 21% helix, 29% strand | Q08285 |
| H | Exosome complex component RRP4 | protein | 291 | 25% helix, 29% strand | P38792 |
| I | Exosome complex component CSL4 | protein | 225 | 4% helix, 44% strand | P53859 |
| J | Exosome complex exonuclease DIS3 (EC 3.1.13.-, 3.1.26.-) | protein | 970 | 34% helix, 25% strand | Q08162 |
| K | Exosome complex exonuclease RRP6 (EC 3.1.13.-) | protein | 576 | 52% helix, 7% strand | Q12149 |
| L | Exosome complex protein LRP1 | protein | 113 | 86% helix, 0% strand | P38801 |
| R | RNA synthetic | rna | 12 | — | — |
| N | RNA synthetic | rna | 6 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1018 | 0.84 | 0.85 | 114 | empty |
| 2 | 320 | 0.80 | 0.91 | 44 | empty |
| 3 | 392 | 0.80 | 0.89 | 51 | empty |
| 4 | 954 | 0.80 | 0.82 | 82 | empty |
| 5 | 881 | 0.79 | 0.82 | 101 | empty |
Interfaces
36 interfaces between chains.
- K–L · 2759 Ų buried · 3 hydrogen bonds · protein-protein
- E–H · 1799 Ų buried · 29 hydrogen bonds · protein-protein
- C–F · 1682 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1571 Ų buried · 23 hydrogen bonds · protein-protein
- B–J · 1537 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 5C0W · Structure of a 12-subunit nuclear exosome complex bound to single-stranded RNA substrates · the same entry in another collection · chain K against K, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q05636
- Every structure of UniProt P46948
- Every structure of UniProt P25359
- Every structure of UniProt P53256
- Every structure of UniProt Q12277
- Every structure of UniProt P48240
- Every structure of UniProt Q08285
- Every structure of UniProt P38792
- Every structure of UniProt P53859
- Every structure of UniProt Q08162
- Every structure of UniProt Q12149
- Every structure of UniProt P38801
- Elsewhere: RCSB PDB 5C0W · PDBe 5C0W · UniProt Q05636 · UniProt P46948 · UniProt P25359 · UniProt P53256 · UniProt Q12277 · UniProt P48240 · UniProt Q08285 · UniProt P38792 · UniProt P53859 · UniProt Q08162 · UniProt Q12149 · UniProt P38801
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