Research workbench
Crystal structure of mouse low-molecular weight protein tyrosine phosphatase type a (lmptp-a) complexed with phosphate
Analyse Crystal structure of mouse low-molecular weight protein tyrosine phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JNU
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Low molecular weight phosphotyrosine protein phosphatase
- EC
- 3.1.3.48
- UniProt
- Q9D358
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Low molecular weight phosphotyrosine protein phosphatase (EC 3.1.3.48) | protein | 153 | 47% helix, 15% strand | Q9D358 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.55 | 0.80 | 34 | empty |
| 2 | 75 | 0.42 | 0.80 | 15 | empty |
| 3 | 99 | 0.37 | 0.75 | 14 | empty |
| 4 | 87 | 0.36 | 0.75 | 20 | empty |
| 5 | 76 | 0.33 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 745 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5JNU · Crystal structure of mouse Low-Molecular Weight Protein Tyrosine Phosphatase type A… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9D358 · AlphaFold monomer V2.0 prediction for low molecular weight phosphotyrosine protein… · 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 Q9D358
- Elsewhere: RCSB PDB 5JNU · PDBe 5JNU · UniProt Q9D358
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