Research workbench
Crystal structure of the N. crassa qde-2 ago mid-piwi domains
Analyse Crystal structure of the N. crassa qde-2 ago mid-piwi domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YHB
- Type
- protein
- Length
- 368 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Post-transcriptional gene silencing protein qde-2
- UniProt
- Q9P8T1
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Post-transcriptional gene silencing protein qde-2 | protein | 368 | 45% helix, 18% strand | Q9P8T1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.59 | 0.78 | 47 | SO4 |
| 2 | 140 | 0.44 | 0.76 | 23 | empty |
| 3 | 115 | 0.36 | 0.73 | 30 | empty |
| 4 | 55 | 0.30 | 0.75 | 14 | empty |
Compared structures
- 2YHB · Crystal Structure of the N. crassa QDE-2 AGO MID-PIWI Domains · 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 Q9P8T1
- Elsewhere: RCSB PDB 2YHB · PDBe 2YHB · UniProt Q9P8T1
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