Research workbench
Human NUDT22
Analyse Human NUDT22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LOU
- Type
- protein
- Length
- 586 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoside diphosphate-linked moiety X motif 22
- UniProt
- Q9BRQ3
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside diphosphate-linked moiety X motif 22 | protein | 285 | 35% helix, 27% strand | Q9BRQ3 |
| B | Nucleoside diphosphate-linked moiety X motif 22 | protein | 301 | 33% helix, 25% strand | Q9BRQ3 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.79 | 0.84 | 84 | PO4 |
| 2 | 475 | 0.72 | 0.82 | 49 | PO4 |
| 3 | 156 | 0.50 | 0.78 | 24 | empty |
| 4 | 57 | 0.47 | 0.85 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 667 Ų buried · 1 hydrogen bond · 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 Q9BRQ3
- Elsewhere: RCSB PDB 5LOU · PDBe 5LOU · UniProt Q9BRQ3
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