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Structure of human prl-3, the phosphatase associated with cancer metastasis

Analyse Structure of human prl-3, the phosphatase associated with cancer metastasis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1V3A
Type
protein
Length
162 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein tyrosine phosphatase type iva
EC
3.1.3.48
UniProt
O75365
Pockets
3 · best druggability 0.58

Structure

solution nmr · 1 distinct chain · 33% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein tyrosine phosphatase type iva (EC 3.1.3.48)protein16233% helix, 12% strandO75365

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12030.580.8042empty
2880.510.8317empty
31020.450.7923empty

Compared structures

  • 1V3A · Structure of human PRL-3, the phosphatase associated with cancer metastasis · the same entry in another collection · chain A against A, TM-score 1.00
  • O75365 · AlphaFold monomer V2.0 prediction for protein tyrosine phosphatase type iva 3 (O75365) · a predicted model of the same protein · chain A against A, TM-score 0.73

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