MolNFT v1 · #18590 · protein

Crystal structure of protein tyrosine phosphatase 1B complexed with two phosphotyrosine molecules

1PTY: “Crystal structure of protein tyrosine phosphatase 1B complexed with two phosphotyrosine molecules”. X-ray diffraction, 2 ligands (PTR, MG), 1 pocket (best druggability 0.51). MolNFT v1 #18590 on GenesisL1: 3D structure, binding…

PDB: 1PTY
Type: protein
Length: 298 residues
Chains: 1
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: PTR, MG
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein tyrosine phosphatase 1B (EC 3.1.3.48)	protein	298	37% helix, 20% strand	P18031

Ligands and binding sites

PTR · O-phosphotyrosine · ligand · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.51	0.86	13	PTR

Compared structures

1PTY · Crystal structure of protein tyrosine phosphatase 1B complexed with two phosphotyrosine… · 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 1PTY · PDBe 1PTY · UniProt P18031

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