MolNFT v2 · #36496 · protein
Protein tyrosine phosphatase 1B with sulfamic acid inhibitors
2F70 · Tyrosine-protein phosphatase, non-receptor type 1: “Protein tyrosine phosphatase 1B with sulfamic acid inhibitors”. X-ray diffraction at 2.12, 3 ligands (UN6, MG, CL). MolNFT v2 #36496 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2F70
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.12
- Source
- Homo sapiens
- Molecule
- Tyrosine-protein phosphatase, non-receptor type 1
- EC
- 3.1.3.48
- UniProt
- P18031
- Ligands
- UN6, MG, CL
Structure
x-ray diffraction · resolution 2.12 · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase, non-receptor type 1 (EC 3.1.3.48) | protein | 297 | 38% helix, 21% strand | P18031 |
Ligands and binding sites
- UN6 · (3-{[3-(3-sulfoamino-phenyl)-propionylamino]-methyl}-phenyl)-sulfamic acid · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2F70 · Protein tyrosine phosphatase 1B with sulfamic acid inhibitors · the same entry in another collection · chain A against A, TM-score 1.00
- P18031 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 1… · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P18031
- Elsewhere: RCSB PDB 2F70 · PDBe 2F70 · UniProt P18031
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.