GL1X · GenesisL1 explorer

UniProt Q86YL7

Putative zinc metalloprotease aq_1964,PA14 from Podoplanin,Putative zinc metalloprotease aq_1964 (Q86YL7)

Putative zinc metalloprotease aq_1964,PA14 from Podoplanin,Putative zinc metalloprotease aq_1964 (UniProt Q86YL7): 9 experimental structures on GenesisL1, 3 ligands bound, 9 pockets. Binding sites, pockets, druggability and 3D…

UniProt
Q86YL7
Protein
Putative zinc metalloprotease aq_1964,PA14 from Podoplanin,Putative zinc…
Experimental structures
9
Predicted models
0
Ligands
3
Pockets
9 · 2 records with a druggable one

Structures

9 records of Q86YL7 in the MolNFT archive: 9 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
3WSRCrystal structure of CLEC-2 in complex with O-glycosylated podoplaninx-ray diffractionC, D——
3WSRCrystal structure of clec-2 in complex with O-glycosylated podoplaninx-ray diffractionC, D——
7C94Crystal structure of the anti-human podoplanin antibody Fab fragment complex with glycopeptidex-ray diffractionC, FA2G, SIA—
7C94Crystal structure of the anti-human podoplanin antibody Fab fragment complex with glycopeptidex-ray diffractionC, FA2G, SIA—
7CQCThe NZ-1 Fab complexed with the PDZ tandem fragment of A. aeolicus S2P homolog with the PA14 tag…x-ray diffractionA—3 (best 0.59)
7CQCThe nz-1 Fab complexed with the PDZ tandem fragment of a. aeolicus S2P homolog with the PA14 tag…x-ray diffractionASNN—
7CQDThe NZ-1 Fab complexed with the PDZ tandem fragment of A. aeolicus S2P homolog with the PA14 tag…x-ray diffractionA, B—6 (best 0.77)
7CQDThe nz-1 Fab complexed with the PDZ tandem fragment of a. aeolicus S2P homolog with the PA14 tag…x-ray diffractionA, B——
Q86YL7AlphaFold monomer V2.0 prediction for podoplanin (Q86YL7)———

Ligands

  • A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · in 2 records
  • SIA · N-acetyl-alpha-neuraminic acid · in 2 records
  • SNN · L-3-aminosuccinimide · in 1 record

Experiment against prediction

Elsewhere

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.