Gamma-tubulin complex component 2 (TUBGCP2) is a 902-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BSJ2.
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The mean pLDDT of this model is 75.6 (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 | 29% |
| 70 to 90 | Confident: backbone generally right | 38% |
| 50 to 70 | Low: treat with caution | 20% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation (PubMed:38305685, PubMed:38609661, PubMed:39321809, PubMed:9566967). The gTuRC regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments, a critical step in centrosome duplication and spindle formation (PubMed:38305685, PubMed:38609661, PubMed:39321809). Plays a role in neuronal migration (PubMed:31630790)
Component of the gamma-tubulin ring complex (gTuRC) consisting of TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6 and gamma-tubulin TUBG1 or TUBG2 (PubMed:9566967, PubMed:39321809, PubMed:38609661, PubMed:38305685). TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6 assemble in a 5:5:2:1:1 stoichiometry; each is associated with a gamma-tubulin, thereby arranging 14 gamma-tubulins in a helical manner…
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8RX1 | EM | 3.57 Å | A/C/E/M/f/k=1-902 |
| 8Q62 | EM | 3.72 Å | A/C/E/G/M=1-902 |
| 6V6B | EM | 3.8 Å | C=1-902 |
| 7AS4 | EM | 4.13 Å | A/C/E/G/M=1-902 |
| 6V6S | EM | 4.3 Å | A/C/E/G/M=1-902 |
| 6X0V | EM | 4.5 Å | F=1-902 |
| 9H9P | EM | 4.5 Å | M=1-902 |
| 9QVN | EM | 4.7 Å | A/C/E/G/M=1-902 |
| 7QJ0 | EM | 5.32 Å | G=1-902 |
| 9QVM | EM | 6.8 Å | A/C/E/G/M=1-902 |
| 7QJ1 | EM | 7.0 Å | G=1-902 |
| 8VRD | EM | 7.0 Å | A/C/E/G/M=1-902 |
| 7QJD | EM | 7.1 Å | A/C/E/G/M=1-902 |
| 7QJ3 | EM | 7.6 Å | G/M=1-902 |
| 8VRJ | EM | 7.7 Å | A/C/E/G/M=1-902 |
| 7QJ6 | EM | 7.8 Å | C/E/G=1-902 |
| 7QJ9 | EM | 8.1 Å | C/E/G=1-902 |
| 8VRK | EM | 8.5 Å | A/C/E/G/M=1-902 |
| 7QJ2 | EM | 8.6 Å | E/G=1-902 |
| 7QJ5 | EM | 8.7 Å | A/C/E/G/M=1-902 |
Showing 20 of 28 experimental structures (best resolution first).
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