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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 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

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