Research workbench
Structure of the LSM657 complex: an assembly intermediate of the LSM1 7 and LSM2 8 rings
Analyse Structure of the LSM657 complex: an assembly intermediate of the LSM1 7 and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SWN
- Type
- protein
- Length
- 874 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- U6 snrna-associated sm-like protein LSM7; U6 snrna-associated sm-like protein LSM5; U6…
- UniProt
- O74499, O42978, Q9UUI1
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 10 distinct chains · 9% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | U6 snrna-associated sm-like protein LSM7 | protein | 68 | 0% helix, 57% strand | O74499 |
| A, P | U6 snrna-associated sm-like protein LSM5 | protein | 76 | 9% helix, 54% strand | O42978 |
| B | U6 snrna-associated sm-like protein LSM6 | protein | 71 | 13% helix, 55% strand | Q9UUI1 |
| F | U6 snrna-associated sm-like protein LSM7 | protein | 78 | 6% helix, 58% strand | O74499 |
| D | U6 snrna-associated sm-like protein LSM5 | protein | 73 | 12% helix, 56% strand | O42978 |
| E, T | U6 snrna-associated sm-like protein LSM6 | protein | 72 | 14% helix, 58% strand | Q9UUI1 |
| O | U6 snrna-associated sm-like protein LSM7 | protein | 67 | 4% helix, 58% strand | O74499 |
| Q | U6 snrna-associated sm-like protein LSM6 | protein | 73 | 12% helix, 52% strand | Q9UUI1 |
| R | U6 snrna-associated sm-like protein LSM7 | protein | 76 | 7% helix, 58% strand | O74499 |
| S | U6 snrna-associated sm-like protein LSM5 | protein | 72 | 13% helix, 57% strand | O42978 |
Ligands and binding sites
- ZN · Zinc ion · metal · 16 copies · chains C, A, B, F, D, E, O, P, Q, R, S, T
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 848 | 0.75 | 0.80 | 103 | empty |
| 2 | 856 | 0.73 | 0.78 | 78 | empty |
| 3 | 233 | 0.60 | 0.80 | 31 | empty |
| 4 | 132 | 0.42 | 0.76 | 19 | empty |
| 5 | 67 | 0.40 | 0.80 | 14 | empty |
Interfaces
14 interfaces between chains.
- O–P · 962 Ų buried · 13 hydrogen bonds · protein-protein
- C–A · 955 Ų buried · 13 hydrogen bonds · protein-protein
- F–D · 930 Ų buried · 11 hydrogen bonds · protein-protein
- R–S · 891 Ų buried · 11 hydrogen bonds · protein-protein
- Q–R · 844 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3SWN · Structure of the LSm657 Complex: An Assembly Intermediate of the LSm1 7 and LSm2 8 Rings · the same entry in another collection · chain T against T, 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 O74499
- Every structure of UniProt O42978
- Every structure of UniProt Q9UUI1
- Elsewhere: RCSB PDB 3SWN · PDBe 3SWN · UniProt O74499 · UniProt O42978 · UniProt Q9UUI1
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