Research workbench
PanDDA analysis group deposition -- Crystal Structure of DCP2 (NUDT20) in complex with NUOOA000023a
Analyse PanDDA analysis group deposition -- Crystal Structure of DCP2 (NUDT20) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5QOP
- Type
- protein
- Length
- 149 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.86
- Source
- Homo sapiens
- Molecule
- DCP2 (NUDT20)
- EC
- 3.6.1.62
- UniProt
- Q8IU60
- Ligands
- LDD
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · resolution 1.86 · 1 distinct chain · 25% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DCP2 (NUDT20) (EC 3.6.1.62) | protein | 149 | 25% helix, 32% strand | Q8IU60 |
Ligands and binding sites
- LDD · (azepan-1-yl)(4-methoxyphenyl)methanone · ligand · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 187 | 0.51 | 0.77 | 28 | LDD |
Compared structures
- 5QOP · Pandda analysis group deposition -- crystal structure of DCP2 (NUDT20) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8IU60 · AlphaFold monomer V2.0 prediction for M7GPPPN-mRNA hydrolase (Q8IU60) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q8IU60
- Elsewhere: RCSB PDB 5QOP · PDBe 5QOP · UniProt Q8IU60
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