Research workbench
Crystal structure of the human protein tyrosine phosphatase PTPN5 (step) in complex with compound 2
Analyse Crystal structure of the human protein tyrosine phosphatase PTPN5 (step) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H8R
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.66
- Source
- Homo sapiens
- Molecule
- Tyrosine-protein phosphatase non-receptor type 5
- EC
- 3.1.3.48
- UniProt
- P54829
- Ligands
- FWB, SO4
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · resolution 1.66 · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 5 (EC 3.1.3.48) | protein | 288 | 40% helix, 19% strand | P54829 |
Ligands and binding sites
- FWB · 3-[(2~{S})-2-azanylpropyl]-5-(trifluoromethyl)phenol · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.49 | 0.80 | 21 | FWB |
| 2 | 60 | 0.31 | 0.76 | 16 | empty |
Compared structures
- 6H8R · Crystal structure of the human protein tyrosine phosphatase PTPN5 (step) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P54829 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 5… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P54829
- Elsewhere: RCSB PDB 6H8R · PDBe 6H8R · UniProt P54829
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