MolNFT v1 · #26017 · protein
Crystal structure of PTPL1 human tyrosine phosphatase mutated in colorectal cancer - evidence for a second phosphotyrosine substrate recognition pocket
1WCH · Protein tyrosine phosphatase, non-receptor type 13: “Crystal structure of PTPL1 human tyrosine phosphatase mutated in colorectal cancer - evidence for a second…”. X-ray diffraction, 1 ligand (PO4), 5 pockets (best druggability…
- PDB
- 1WCH
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein tyrosine phosphatase, non-receptor type 13
- EC
- 3.1.3.48
- UniProt
- Q12923
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein tyrosine phosphatase, non-receptor type 13 (EC 3.1.3.48) | protein | 308 | 36% helix, 20% strand | Q12923 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.43 | 0.76 | 19 | empty |
| 2 | 96 | 0.41 | 0.78 | 17 | empty |
| 3 | 146 | 0.39 | 0.73 | 25 | empty |
| 4 | 51 | 0.31 | 0.77 | 18 | empty |
| 5 | 60 | 0.30 | 0.74 | 13 | empty |
Compared structures
- 1WCH · Crystal structure of PTPL1 human tyrosine phosphatase mutated in colorectal cancer… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12923 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 13… · 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 Q12923
- Elsewhere: RCSB PDB 1WCH · PDBe 1WCH · UniProt Q12923
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