Research workbench
Crystal structure of the phosphatase domain of human ptp ia-2
Analyse Crystal structure of the phosphatase domain of human ptp ia-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I1Y
- Type
- protein
- Length
- 577 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase
- EC
- 3.1.3.48
- UniProt
- Q16849
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase (EC 3.1.3.48) | protein | 287 | 37% helix, 20% strand | Q16849 |
| B | Receptor-type tyrosine-protein phosphatase (EC 3.1.3.48) | protein | 290 | 36% helix, 19% strand | Q16849 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 500 | 0.73 | 0.82 | 34 | empty |
| 2 | 650 | 0.67 | 0.76 | 74 | empty |
| 3 | 82 | 0.43 | 0.80 | 14 | GOL |
| 4 | 108 | 0.38 | 0.75 | 19 | empty |
| 5 | 73 | 0.32 | 0.74 | 14 | GOL |
Interfaces
1 interface between chains.
- A–B · 883 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 2I1Y · Crystal structure of the phosphatase domain of human PTP IA-2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q16849 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase-like N… · a predicted model of the same protein · chain B 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 Q16849
- Elsewhere: RCSB PDB 2I1Y · PDBe 2I1Y · UniProt Q16849
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