Research workbench
Crystal structure of the minimal DENR-MCTS1 complex
Analyse Crystal structure of the minimal DENR-MCTS1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ONS
- Type
- protein
- Length
- 205 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.14
- Source
- Homo sapiens
- Molecule
- Malignant T-cell-amplified sequence 1; Density-regulated protein
- UniProt
- Q9ULC4, O43583
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · resolution 2.14 · 2 distinct chains · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Malignant T-cell-amplified sequence 1 | protein | 181 | 34% helix, 29% strand | Q9ULC4 |
| B | Density-regulated protein | protein | 24 | 13% helix, 8% strand | O43583 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.41 | 0.77 | 21 | GOL |
Interfaces
1 interface between chains.
- A–B · 816 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5ONS · Crystal structure of the minimal denr-MCTS1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ULC4 · AlphaFold monomer V2.0 prediction for malignant T-cell-amplified sequence 1 (Q9ULC4) · a predicted model of the same protein · chain A against A, TM-score 0.99
- O43583 · AlphaFold monomer V2.0 prediction for density-regulated protein (O43583) · a predicted model of the same protein · chain B against A, TM-score 0.65
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 Q9ULC4
- Every structure of UniProt O43583
- Elsewhere: RCSB PDB 5ONS · PDBe 5ONS · UniProt Q9ULC4 · UniProt O43583
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