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Crystal structure of the PTPN2 C216G mutant
Analyse Crystal structure of the PTPN2 C216G mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZZ4
- Type
- protein
- Length
- 556 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 2
- EC
- 3.1.3.48
- UniProt
- P17706
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 2 (EC 3.1.3.48) | protein | 279 | 37% helix, 23% strand | P17706 |
| B | Tyrosine-protein phosphatase non-receptor type 2 (EC 3.1.3.48) | protein | 277 | 36% helix, 23% strand | P17706 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.78 | 0.84 | 50 | PO4 |
| 2 | 281 | 0.56 | 0.76 | 33 | empty |
| 3 | 79 | 0.33 | 0.75 | 16 | empty |
| 4 | 55 | 0.32 | 0.77 | 15 | empty |
| 5 | 68 | 0.28 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 767 Ų buried · 12 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 P17706
- Elsewhere: RCSB PDB 6ZZ4 · PDBe 6ZZ4 · UniProt P17706
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