Research workbench
The solution structure of the dm DCP1 EVH1 domain in complex with the XRN1 dbm peptide
Analyse The solution structure of the dm DCP1 EVH1 domain in complex with the XRN1 dbm… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LYD
- Type
- protein
- Length
- 172 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Decapping protein 1; Pacman protein
- UniProt
- Q9W1H5, Q9XZU2
- Pockets
- 1 · best druggability 0.76
Structure
solution nmr · 2 distinct chains · 26% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Decapping protein 1 | protein | 134 | 25% helix, 46% strand | Q9W1H5 |
| B | Pacman protein | protein | 38 | 29% helix, 0% strand | Q9XZU2 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.76 | 0.94 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 779 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2LYD · The solution structure of the Dm DCP1 EVH1 domain in complex with the XRN1 DBM peptide · the same entry in another collection · chain A against A, 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 Q9W1H5
- Every structure of UniProt Q9XZU2
- Elsewhere: RCSB PDB 2LYD · PDBe 2LYD · UniProt Q9W1H5 · UniProt Q9XZU2
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