Research workbench
Engineered catalytic domain of protein tyrosine phosphatase hptpbeta.
Analyse Engineered catalytic domain of protein tyrosine phosphatase hptpbeta. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HC1
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase beta
- EC
- 3.1.3.48
- UniProt
- P23467
- Ligands
- CL
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase beta (EC 3.1.3.48) | protein | 290 | 36% helix, 21% strand | P23467 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.50 | 0.78 | 22 | empty |
| 2 | 84 | 0.31 | 0.73 | 19 | CL |
Compared structures
- 2HC1 · Engineered catalytic domain of protein tyrosine phosphatase HPTPbeta. · the same entry in another collection · chain A against A, TM-score 1.00
- P23467 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase beta… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P23467
- Elsewhere: RCSB PDB 2HC1 · PDBe 2HC1 · UniProt P23467
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