Research workbench
Crystal structure of putative ADP ribose pyrophosphatase
Analyse Crystal structure of putative ADP ribose pyrophosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VIQ
- Type
- protein
- Length
- 599 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribose pyrophosphatase
- EC
- 3.6.1.13
- UniProt
- Q93K97
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 27% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribose pyrophosphatase (EC 3.6.1.13) | protein | 204 | 25% helix, 39% strand | Q93K97 |
| B | ADP-ribose pyrophosphatase (EC 3.6.1.13) | protein | 201 | 27% helix, 39% strand | Q93K97 |
| C | ADP-ribose pyrophosphatase (EC 3.6.1.13) | protein | 194 | 28% helix, 38% strand | Q93K97 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.70 | 0.84 | 42 | empty |
| 2 | 297 | 0.69 | 0.83 | 43 | empty |
| 3 | 371 | 0.63 | 0.78 | 53 | empty |
| 4 | 246 | 0.51 | 0.76 | 36 | empty |
| 5 | 83 | 0.41 | 0.78 | 17 | empty |
Interfaces
3 interfaces between chains.
- B–C · 3835 Ų buried · 50 hydrogen bonds · protein-protein
- A–B · 418 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 82 Ų buried · 0 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 Q93K97
- Elsewhere: RCSB PDB 1VIQ · PDBe 1VIQ · UniProt Q93K97
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