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Crystal structure of the tho-SUB2 complex
Analyse Crystal structure of the tho-SUB2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SUQ
- Type
- protein
- Length
- 5,585 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent RNA helicase SUB2; TEX1; THO2, HPR1, MFT1, and THP2
- EC
- 3.6.4.13
- UniProt
- Q07478
- Ligands
- KEG
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 82% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | ATP-dependent RNA helicase SUB2 (EC 3.6.4.13) | protein | 374 | 42% helix, 18% strand | Q07478 |
| B, D | TEX1 | protein | 188 | 0% helix, 60% strand | — |
| M | THO2, HPR1, MFT1, and THP2 | protein | 2231 | 88% helix, 0% strand | — |
| N | THO2, HPR1, MFT1, and THP2 | protein | 2230 | 88% helix, 0% strand | — |
Ligands and binding sites
- KEG · 12-tungstophosphate · ligand · 11 copies · chains A, C, M, N
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 | 694 | 0.73 | 0.79 | 55 | empty |
| 2 | 890 | 0.70 | 0.76 | 78 | empty |
| 3 | 492 | 0.70 | 0.80 | 71 | empty |
| 4 | 1178 | 0.69 | 0.74 | 114 | empty |
| 5 | 1078 | 0.69 | 0.74 | 105 | empty |
Interfaces
7 interfaces between chains.
- C–N · 1058 Ų buried · 8 hydrogen bonds · protein-protein
- A–M · 949 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 786 Ų buried · 36 hydrogen bonds · protein-protein
- C–M · 193 Ų buried · 0 hydrogen bonds · protein-protein
- A–N · 186 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 covalent, 1 isopeptide (covalent ligand, isopeptide).
Compared structures
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 Q07478
- Elsewhere: RCSB PDB 5SUQ · PDBe 5SUQ · UniProt Q07478
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