Charged multivesicular body protein 1b (CHMP1B) is a 199-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q7LBR1.
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The mean pLDDT of this model is 80.8 (confident 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 | 44% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 16% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is…
Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with CHMP1A. Interacts with VTA1; the interaction probably involves the open…
Cytoplasm, cytosol, Endosome, Late endosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4TXR | X-ray | 1.0 Å | B=176-199 |
| 4TXQ | X-ray | 2.21 Å | C/D=176-199 |
| 3EAB | X-ray | 2.5 Å | G/H/I/J/K/L=148-197 |
| 8V2S | EM | 2.72 Å | A=1-199 |
| 6E8G | EM | 2.9 Å | AA/AB/B/CA/CB/D/EA/EB/F/GA/GB/H/IA/IB/J/KA/KB/L/MA/MB/N/OA/OB/P/QA/QB/R/SA/SB/T=1-199 |
| 8V2Q | EM | 2.95 Å | A=1-199 |
| 8V2R | EM | 3.01 Å | A=1-199 |
| 6TZ5 | EM | 3.1 Å | AA/AB/B/CA/CB/D/EA/EB/F/GA/GB/H/IA/IB/J/KA/KB/L/MA/MB/N/OA/OB/P/QA/QB/R/SA/T/UA=1-199 |
| 6TZ4 | EM | 3.2 Å | 02/A/BA/BB/C/DA/DB/E/FA/FB/G/HA/HB/I/JA/JB/K/LA/LB/M/NA/NB/O/PA/PB/Q/RA/RB/S/TA=1-199 |
| 3JC1 | EM | 4.0 Å | Ab/Ad/Af/Ah/Aj/Al/An/Ap/Ar/At/Av/Ax/Az/Bb/Bd/Bf/Bh/Bj/Bl/Bn/Bp/Br/Bt/Bv/Bx/Bz/Cb/Cd/Cf/Ch=4-163 |
| 6TZ9 | EM | 6.2 Å | A/AA/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y/Z=1-199 |
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