GL1X · GenesisL1 explorer

UniProt O59196

Tetrahedral aminopeptidase (O59196)

Tetrahedral aminopeptidase (UniProt O59196), EC 3.4.11.-: 11 experimental structures on GenesisL1, 1 ligand bound, 24 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
O59196
Protein
Tetrahedral aminopeptidase
EC
3.4.11.-
Experimental structures
11
Predicted models
0
Ligands
1
Pockets
24 · 1 record with a druggable one

Structures

11 records of O59196 in the MolNFT archive: 11 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1XFOCrystal Structure of an archaeal aminopeptidasex-ray diffractionA, B, C, D——
1XFOCrystal structure of an archaeal aminopeptidasex-ray diffractionA, B, C, D——
1Y0RCrystal structure of the tetrahedral aminopeptidase from P. horikoshiix-ray diffractionA——
1Y0RCrystal structure of the tetrahedral aminopeptidase from P. horikoshiix-ray diffractionA——
1Y0YCrystal structure of tetrahedral aminopeptidase from P. horikoshii in complex with amastatinx-ray diffractionA——
1Y0YCrystal structure of tetrahedral aminopeptidase from P. horikoshii in complex with amastatinx-ray diffractionA——
6F3KCombined solid-state NMR, solution-state NMR and EM data for structure determination of the…electron microscopy, solution nmr, solid-state nmrAZN4 (best 0.38)
6F3KCombined solid-state NMR, solution-state NMR and EM data for structure determination of the…electron microscopy; solution nmr; solid-state nmrAZN—
6R8NStructure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii by use of…electron microscopy, solution nmrA, B, C, D, E, F, G, H, I, J, K, LZN20 (best 0.84)
6R8NStructure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii by use of…electron microscopy; solution nmrA, B, C, D, E, F, G, H, I, J, K, LZN—
O59196AlphaFold monomer V2.0 prediction for tetrahedral aminopeptidase (O59196)———

Ligands

  • ZN · Zinc ion · in 4 records

Elsewhere

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