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Crystal structure of mid domain from HAGO2
Analyse Crystal structure of mid domain from HAGO2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LUC
- Type
- protein
- Length
- 401 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein argonaute-2
- UniProt
- Q9UKV8
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein argonaute-2 | protein | 135 | 48% helix, 16% strand | Q9UKV8 |
| B, C | Protein argonaute-2 | protein | 133 | 48% helix, 17% strand | Q9UKV8 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 8 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.41 | 0.78 | 19 | empty |
| 2 | 59 | 0.35 | 0.78 | 17 | PO4 |
| 3 | 79 | 0.32 | 0.74 | 20 | empty |
| 4 | 56 | 0.29 | 0.75 | 11 | empty |
Interfaces
2 interfaces between chains.
- B–C · 702 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 677 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
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 Q9UKV8
- Elsewhere: RCSB PDB 3LUC · PDBe 3LUC · UniProt Q9UKV8
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