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AlphaFold monomer V2.0 prediction for 30S ribosomal protein S15, chloroplastic (B2LMP1)

Analyse AlphaFold monomer V2.0 prediction for 30S ribosomal protein S15, chloroplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B2LMP1
Type
protein
Length
92 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x694B2EBF0D3E528C389146c9d11396619e7466a9
Molecule
30S ribosomal protein S15, chloroplastic
UniProt
B2LMP1

Structure

1 distinct chain · 73% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A30S ribosomal protein S15, chloroplasticprotein9273% helix, 0% strandB2LMP1

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