GL1X · GenesisL1 explorer

UniProt Q03689

Q03689

Q03689 (UniProt Q03689): 13 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q03689
Experimental structures
13
Predicted models
0

Structures

13 records of Q03689 in the MolNFT archive: 13 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
2KJ3High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state…solid-state nmrA, B, C——
2KJ3High-resolution structure of the het-S(218-289) prion in its amyloid form obtained by solid-state…solid-state nmrA, B, C——
2LBUHADDOCK calculated model of Congo red bound to the HET-s amyloidsolid-state nmrA, B, C, D, E——
2LBUHaddock calculated model of congo red bound to the het-S amyloidsolid-state nmrA, B, C, D, E——
2MUSHADDOCK calculated model of LIN5001 bound to the HET-s amyloidsolution nmrA, B, C, D, E——
2MUSHaddock calculated model of LIN5001 bound to the het-S amyloidsolution nmrA, B, C, D, E——
2RNMStructure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMRsolution nmrA, B, C, D, E——
2RNMStructure of the het-S(218-289) prion in its amyloid form obtained by solid-state NMRsolution nmrA, B, C, D, E——
2WVNStructure of the HET-s N-terminal domainx-ray diffractionA——
2WVNStructure of the het-S N-terminal domainx-ray diffractionA——
2WVQStructure of the HET-s N-terminal domain. Mutant D23A, P33Hx-ray diffractionA, B——
2WVQStructure of the het-S N-terminal domain. mutant D23A, P33Hx-ray diffractionA, B——
Q03689AlphaFold monomer V2.0 prediction for heterokaryon incompatibility protein S (Q03689)———

Elsewhere

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