Research workbench
Crystal structure of yersinia protein tyrosine phosphatase at 2.5 ångströms and the complex with tungstate
Analyse Crystal structure of yersinia protein tyrosine phosphatase at 2.5 ångströms and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YPT
- Type
- protein
- Length
- 558 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-tyrosine phosphatase yersinia (catalytic domain)
- EC
- 3.1.3.48
- UniProt
- P15273
- Pockets
- 8 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-tyrosine phosphatase yersinia (catalytic domain) (EC 3.1.3.48) | protein | 278 | 38% helix, 21% strand | P15273 |
| B | Protein-tyrosine phosphatase yersinia (catalytic domain) (EC 3.1.3.48) | protein | 280 | 38% helix, 21% strand | P15273 |
Pockets
8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.49 | 0.77 | 24 | empty |
| 2 | 227 | 0.48 | 0.74 | 39 | empty |
| 3 | 172 | 0.48 | 0.77 | 22 | empty |
| 4 | 125 | 0.45 | 0.78 | 22 | empty |
| 5 | 123 | 0.45 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 472 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1YPT · Crystal structure of yersinia protein tyrosine phosphatase at 2.5 ångströms and the… · the same entry in another collection · chain B against B, TM-score 1.00
- P15273 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase yoph (P15273) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P15273
- Elsewhere: RCSB PDB 1YPT · PDBe 1YPT · UniProt P15273
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