GL1X · GenesisL1 explorer

UniProt P17198

30S ribosomal protein S7 (P17198)

30S ribosomal protein S7 (UniProt P17198): 11 experimental structures and 1 predicted model on GenesisL1, 24 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P17198
Protein
30S ribosomal protein S7
Experimental structures
11
Predicted models
1
Pockets
24 · 10 records with a druggable one

Structures

12 records of P17198 in the MolNFT archive: 11 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
8HKXCryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosomeelectron microscopyAS7P—4 (best 0.86)
8HKYCryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosomeelectron microscopyAS7P—1 (best 0.88)
8HKZCryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosomeelectron microscopyAS7P—2 (best 0.89)
8HL1Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosomeelectron microscopyAS7P—1 (best 0.87)
8HL2Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosomeelectron microscopyAS7P——
8HL3Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosomeelectron microscopyAS7P—1 (best 0.85)
8HL4Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosomeelectron microscopyAS7P—3 (best 0.86)
8HL5Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosomeelectron microscopyAS7P—1 (best 0.84)
8WKPStructural basis of translation inhibition by a valine tRNA-derived fragmentelectron microscopyAS7P—3 (best 0.88)
8WQ2Structural basis of translation inhibition by a valine tRNA-derived fragmentelectron microscopyAS7P—3 (best 0.87)
8WQ4Structural basis of translation inhibition by a valine tRNA-derived fragmentelectron microscopyAS7P—3 (best 0.87)
P17198AlphaFold monomer V2.0 prediction for 30S ribosomal protein S7 (P17198)predictedA—2 (best 0.41)

Experiment against prediction

Elsewhere

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