Research workbench
Protein tyrosine phosphatase 1B with sulfamic acid inhibitors
Analyse Protein tyrosine phosphatase 1B with sulfamic acid inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F70
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase, non-receptor type 1
- EC
- 3.1.3.48
- UniProt
- P18031
- Ligands
- UN6, MG, CL
Structure
x-ray diffraction · 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
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
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