MolNFT v2 · #129966 · protein
Crystal structure of the minimal DENR-MCTS1 complex
5ONS: “Crystal structure of the minimal DENR-MCTS1 complex”. X-ray diffraction at 2.14, 1 ligand (ZN). MolNFT v2 #129966 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- Q9ULC4, O43583
- Ligands
- ZN
Structure
x-ray diffraction · resolution 2.14 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 181 | — | Q9ULC4 |
| B | — | protein | 24 | — | O43583 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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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