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UniProt P21465

30S ribosomal protein S3 (P21465)

30S ribosomal protein S3 (UniProt P21465): 15 experimental structures on GenesisL1, 16 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P21465
Protein
30S ribosomal protein S3
Experimental structures
15
Predicted models
0
Pockets
16 · 8 records with a druggable one

Structures

15 records of P21465 in the MolNFT archive: 15 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
3J9WCryo-EM structure of the Bacillus subtilis MifM-stalled ribosome complexelectron microscopyAC——
5NJTStructure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization.electron microscopyC——
6HA1Cryo-EM structure of a 70S Bacillus subtilis ribosome translating the ErmD leader peptide in…electron microscopyc——
6HA8Cryo-EM structure of the ABCF protein VmlR bound to the Bacillus subtilis ribosomeelectron microscopyc——
6HTQStringent response control by a bifunctional RelA enzyme in the presence and absence of the ribosomeelectron microscopyc——
7O5BCryo-EM structure of a Bacillus subtilis MifM-stalled ribosome-nascent chain complex with…electron microscopyC—3 (best 0.85)
7QV1Bacillus subtilis collided disome (Leading 70S)electron microscopyc—2 (best 0.84)
7QV2Bacillus subtilis collided disome (Collided 70S)electron microscopyc—2 (best 0.84)
7QV3Bacillus subtilis MutS2-collided disome complex (MutS2 conf.2; Leading 70S)electron microscopyc—2 (best 0.84)
8BUUARE-ABCF VmlR2 bound to a 70S ribosomeelectron microscopyc—2 (best 0.84)
8CDURnase R bound to a 30S degradation intermediate (main state)electron microscopyE—3 (best 0.86)
8CECRnase R bound to a 30S degradation intermediate (State I - head-turning)electron microscopyH—1 (best 0.77)
8CEDRnase R bound to a 30S degradation intermediate (State I - head-turning)electron microscopyE—1 (best 0.78)
8CEERnase R bound to a 30S degradation intermediate (State I - head-turning)electron microscopyE——
P21465AlphaFold monomer V2.0 prediction for 30S ribosomal protein S3 (P21465)———

Elsewhere

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