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Crystal structure of TYR/SER protein phosphatase from vaccinia virus wr
Analyse Crystal structure of TYR/SER protein phosphatase from vaccinia virus wr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q05
- Type
- protein
- Length
- 713 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein phosphatase
- EC
- 3.1.3.48, 3.1.3.16
- UniProt
- P07239
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 43% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein phosphatase (EC 3.1.3.48, 3.1.3.16) | protein | 181 | 42% helix, 10% strand | P07239 |
| B | Dual specificity protein phosphatase (EC 3.1.3.48, 3.1.3.16) | protein | 179 | 44% helix, 11% strand | P07239 |
| C | Dual specificity protein phosphatase (EC 3.1.3.48, 3.1.3.16) | protein | 172 | 44% helix, 11% strand | P07239 |
| D | Dual specificity protein phosphatase (EC 3.1.3.48, 3.1.3.16) | protein | 181 | 42% helix, 10% strand | P07239 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 833 | 0.78 | 0.81 | 77 | empty |
| 2 | 162 | 0.58 | 0.82 | 22 | empty |
| 3 | 327 | 0.51 | 0.73 | 51 | empty |
| 4 | 52 | 0.49 | 0.86 | 16 | empty |
| 5 | 56 | 0.45 | 0.83 | 18 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1183 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 1145 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 418 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 340 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 338 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 modified (engineered).
Compared structures
- 2Q05 · Crystal structure of tyr/ser protein phosphatase from Vaccinia virus WR · 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 P07239
- Elsewhere: RCSB PDB 2Q05 · PDBe 2Q05 · UniProt P07239
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