Large ribosomal subunit protein bL34 (rpmH) is a 47-residue protein from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9RSH2.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 95.4 (very high overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 89% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Binds the 23S rRNA
Part of the 50S ribosomal subunit. Contacts protein L4
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5DM6 | X-ray | 2.9 Å | 2=1-47 |
| 2ZJR | X-ray | 2.91 Å | 2=1-47 |
| 5DM7 | X-ray | 3.0 Å | 2=1-47 |
| 1NKW | X-ray | 3.1 Å | 2=1-47 |
| 4IO9 | X-ray | 3.2 Å | 2=1-47 |
| 4IOA | X-ray | 3.2 Å | 2=1-47 |
| 7A0S | X-ray | 3.22 Å | 2=1-47 |
| 3PIO | X-ray | 3.25 Å | 2=1-47 |
| 1NWY | X-ray | 3.3 Å | 2=1-47 |
| 2ZJQ | X-ray | 3.3 Å | 2=1-47 |
| 3CF5 | X-ray | 3.3 Å | 2=1-47 |
| 7A0R | X-ray | 3.3 Å | 2=1-47 |
| 7A18 | X-ray | 3.4 Å | 2=1-46 |
| 1SM1 | X-ray | 3.42 Å | 2=1-47 |
| 5JVG | X-ray | 3.43 Å | 2=1-47 |
| 3PIP | X-ray | 3.45 Å | 2=1-47 |
| 1NWX | X-ray | 3.5 Å | 2=1-47 |
| 1XBP | X-ray | 3.5 Å | 2=1-47 |
| 3DLL | X-ray | 3.5 Å | 2=1-47 |
| 4WFN | X-ray | 3.54 Å | 2=1-47 |
Showing 20 of 31 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.