Research workbench
AlphaFold monomer V2.0 prediction for 50S ribosomal protein L15 (Q1R630)
Analyse AlphaFold monomer V2.0 prediction for 50S ribosomal protein L15 (Q1R630) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1R630
- Type
- protein
- Length
- 144 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79C8eac7b0A7F48c5Dc63A746EA9A516335a21cf
- Molecule
- 50S ribosomal protein L15
- UniProt
- Q1R630
Structure
1 distinct chain · 25% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L15 | protein | 144 | 25% helix, 15% strand | Q1R630 |
Compared structures
- 8FZD · Cryo-EM structure of an E. coli non-rotated ribosome termination complex bound with… · an experimental structure of the same protein · chain A against N, TM-score 0.88
- 8FZI · Cryo-EM structure of an E. coli rotated ribosome bound with RF3-GDPCP and p/E-tRNAPhe… · an experimental structure of the same protein · chain A against N, TM-score 0.88
- 8FZG · Cryo-EM structure of an E. coli non-rotated ribosome termination complex bound with… · an experimental structure of the same protein · chain A against N, TM-score 0.87
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q1R630
- Elsewhere: UniProt Q1R630 · AlphaFold DB Q1R630
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