Research workbench
Crystal structure of a novel phosphatase from deinococcus radiodurans
Analyse Crystal structure of a novel phosphatase from deinococcus radiodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T70
- Type
- protein
- Length
- 2,040 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatase
- UniProt
- Q9RUV0
- Pockets
- 15 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Phosphatase | protein | 255 | 24% helix, 31% strand | Q9RUV0 |
Pockets
15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 738 | 0.74 | 0.79 | 87 | empty |
| 2 | 1033 | 0.74 | 0.77 | 87 | empty |
| 3 | 63 | 0.73 | 0.98 | 19 | empty |
| 4 | 705 | 0.72 | 0.78 | 73 | empty |
| 5 | 55 | 0.70 | 0.98 | 17 | empty |
Interfaces
12 interfaces between chains.
- C–D · 1710 Ų buried · 23 hydrogen bonds · protein-protein
- G–H · 1703 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1698 Ų buried · 31 hydrogen bonds · protein-protein
- E–F · 1696 Ų buried · 25 hydrogen bonds · protein-protein
- D–E · 716 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1T70 · Crystal structure of a novel phosphatase from Deinococcus radiodurans · the same entry in another collection · chain H against H, TM-score 1.00
- Q9RUV0 · AlphaFold monomer V2.0 prediction for PHOSPHATASE/PHOSPHODIESTERASE DR_1281 (Q9RUV0) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9RUV0
- Elsewhere: RCSB PDB 1T70 · PDBe 1T70 · UniProt Q9RUV0
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