MolNFT v1 · #101845 · protein
Tandem chromodomains of human CHD1 in complex with influenza NS1 C- terminal tail dimethylated at K229
4O42 · Chromodomain-helicase-DNA-binding protein 1: “Tandem chromodomains of human CHD1 in complex with influenza NS1 C- terminal tail dimethylated at K229”. X-ray diffraction, 1 ligand (UNX), 2 pockets (best druggability 0.43). MolNFT v1…
- PDB
- 4O42
- Type
- protein
- Length
- 180 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromodomain-helicase-DNA-binding protein 1; Nonstructural protein 1
- EC
- 3.6.4.12
- UniProt
- O14646, Q38SQ2
- Ligands
- UNX
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chromodomain-helicase-DNA-binding protein 1 (EC 3.6.4.12) | protein | 173 | 44% helix, 24% strand | O14646 |
| B | Nonstructural protein 1 | protein | 7 | 0% helix, 0% strand | Q38SQ2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.43 | 0.76 | 19 | empty |
| 2 | 52 | 0.34 | 0.78 | 17 | UNX, GOL |
Interfaces
1 interface between chains.
- A–B · 548 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 4O42 · Tandem chromodomains of human CHD1 in complex with influenza NS1 C-terminal tail… · the same entry in another collection · chain A against A, TM-score 1.00
- O14646 · AlphaFold monomer V2.0 prediction for chromodomain-helicase-DNA- binding protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O14646
- Every structure of UniProt Q38SQ2
- Elsewhere: RCSB PDB 4O42 · PDBe 4O42 · UniProt O14646 · UniProt Q38SQ2
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