Research workbench
Crystal structure of human tyrosine phosphatase shp-1
Analyse Crystal structure of human tyrosine phosphatase shp-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B3O
- Type
- protein
- Length
- 504 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase, non-receptor type 6
- EC
- 3.1.3.48
- UniProt
- P29350
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase, non-receptor type 6 (EC 3.1.3.48) | protein | 504 | 27% helix, 23% strand | P29350 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1028 | 0.76 | 0.79 | 66 | empty |
| 2 | 93 | 0.65 | 0.91 | 36 | empty |
| 3 | 109 | 0.42 | 0.77 | 22 | empty |
| 4 | 77 | 0.42 | 0.80 | 13 | empty |
| 5 | 50 | 0.33 | 0.78 | 14 | empty |
Compared structures
- 2B3O · Crystal structure of human tyrosine phosphatase SHP-1 · the same entry in another collection · chain A against A, TM-score 1.00
- P29350 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 6… · a predicted model of the same protein · chain A against A, TM-score 0.64
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 P29350
- Elsewhere: RCSB PDB 2B3O · PDBe 2B3O · UniProt P29350
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.