Research workbench
Crystal structure of Low Molecular Weight Protein Tyrosine Phosphatase isoform A complexed with phenylmethanesulfonic acid
Analyse Crystal structure of Low Molecular Weight Protein Tyrosine Phosphatase isoform… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Z9A
- Type
- protein
- Length
- 154 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Homo sapiens
- Molecule
- Low molecular weight phosphotyrosine protein phosphatase
- EC
- 3.1.3.48, 3.1.3.2
- UniProt
- P24666
- Ligands
- PMS, SO4
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Low molecular weight phosphotyrosine protein phosphatase (EC 3.1.3.48, 3.1.3.2) | protein | 154 | 44% helix, 15% strand | P24666 |
Ligands and binding sites
- PMS · phenylmethanesulfonic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.35 | 0.78 | 12 | PMS |
Compared structures
- 4Z9A · Crystal structure of low molecular weight protein tyrosine phosphatase isoform a… · the same entry in another collection · chain A against A, TM-score 1.00
- P24666 · 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 P24666
- Elsewhere: RCSB PDB 4Z9A · PDBe 4Z9A · UniProt P24666
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