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Crystal structure of the PTP1B complexed with SP7343-SP7964, a ptyr mimetic

Analyse Crystal structure of the PTP1B complexed with SP7343-SP7964, a ptyr mimetic in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NWL
Type: protein
Length: 283 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-tyrosine phosphatase, non-receptor type 1
EC: 3.1.3.48
UniProt: P18031
Ligands: 964, MG
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-tyrosine phosphatase, non-receptor type 1 (EC 3.1.3.48)	protein	283	36% helix, 23% strand	P18031

Ligands and binding sites

964 · 3-(4-{2-[2-(2-bromo-acetylamino)-ethyldisulfanyl]-ethylcarbamoyl}-cyclohexylcarbamoyl)-pyrazine-2-carboxylic acid · ligand · chains A
MG · Magnesium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	165	0.46	0.76	24	964

Compared structures

1NWL · Crystal structure of the PTP1B complexed with SP7343-SP7964, a pTyr mimetic · 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 1NWL · PDBe 1NWL · UniProt P18031

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