P23258: Tubulin gamma-1 chain (TUBG1)

Tubulin gamma-1 chain (TUBG1) is a 451-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P23258.

Gene
TUBG1
Organism
Homo sapiens
Length
451 residues
Mean pLDDT
91.6
Model
AF-P23258-F1 v6
Model created
1 Aug 2025
PDB structures
32

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.6 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate77%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:38305685, PubMed:38609661, PubMed:39321809). Gamma-tubulin is a key component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation (PubMed:38305685, PubMed:38609661, PubMed:39321809). 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 sperm morphological development during late stage spermiogenesis, particularly the anchoring of the…

Subunit structure

Component of the gamma-tubulin ring complex (gTuRC) consisting of TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6 and gamma-tubulin TUBG1 or TUBG2 (PubMed:9566969, 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…

Subcellular location

Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cytoskeleton, spindle

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3CB2X-ray2.3 ÅA/B=1-451
1Z5VX-ray2.71 ÅA=1-449
1Z5WX-ray3.0 ÅA=1-449
8RX1EM3.57 Å1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451
8Q62EM3.72 Åa/b/c/d/e/f/g/h/i/j/k/l/m/n=1-451
6V5VEM3.8 Åg=1-451
7AS4EM4.13 Å1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-447
6V6SEM4.3 Åa/b/c/d/e/f/g/h/i/j/k/l/m/t=1-451
8VA2EM4.5 Åg/h=1-441
9H9PEM4.5 Ål/m=1-451
9QVNEM4.7 Åa/b/c/d/e/f/g/h/i/j/k/l/m/n=1-451
7QJ0EM5.32 ÅU/V/W/X/Y/Z=1-451
9QVMEM6.8 Åa/b/c/d/e/f/g/h/i/j/k/l/m/n=1-451
7QJ1EM7.0 ÅU/V/W/X/Y/Z=1-451
8VRDEM7.0 Åa/b/c/d/e/f/g/h/i/j/k/l/m/n=1-451
7QJDEM7.1 Å1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451
7QJ3EM7.6 Å1/2/U/V/W/X/Y/Z=1-451
8VRJEM7.7 Åa/b/c/d/e/f/g/h/i/j/k/l/m/n=1-451
7QJ6EM7.8 ÅQ/R/S/T/U/V/W/X/Y/Z=1-451
7QJEEM7.8 ÅW/X/Y/Z=1-451

Showing 20 of 32 experimental structures (best resolution first).

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