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Human PTP1B catalytic domain complexed with PNU177836

Analyse Human PTP1B catalytic domain complexed with PNU177836 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JF7
Type: protein
Length: 562 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-tyrosine phosphatase 1B
EC: 3.1.3.48
UniProt: P18031
Ligands: TBH
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein-tyrosine phosphatase 1B (EC 3.1.3.48)	protein	281	35% helix, 23% strand	P18031

Ligands and binding sites

TBH · 5-(2-{2-[(tert-butoxy-hydroxy-methyl)-amino]-1-hydroxy-3-phenyl-propylamino}-3-hydroxy-3-pentylamino-propyl)-2-carboxymethoxy-benzoic acid · ligand · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1074	0.79	0.80	78	TBH
2	86	0.34	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 430 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1JF7 · Human PTP1B catalytic domain complexed with PNU177836 · 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 1JF7 · PDBe 1JF7 · UniProt P18031

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