Clathrin heavy chain 1 (CLTC) is a 1675-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49951.
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The mean pLDDT of this model is 75.8 (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 | 10% |
| 70 to 90 | Confident: backbone generally right | 63% |
| 50 to 70 | Low: treat with caution | 23% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Plays a role in early autophagosome formation. Interaction with DNAJC6 mediates the recruitment of HSPA8 to the clathrin lattice and creates local destabilization of the lattice promoting uncoating…
Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat. In the presence of light chains, hub assembly is influenced by both the pH and the concentration of calcium. Interacts with HIP1. Interacts with DENND1A, DENND1B and DENND1C. Interacts with OCRL. Interacts with ERBB2. Interacts with FKBP6 (By similarity). Interacts with CKAP5 and…
Cytoplasmic vesicle membrane, Membrane, coated pit, Melanosome, Cytoplasm, cytoskeleton, spindle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5M5T | X-ray | 1.7 Å | A/B=1-363 |
| 9F8T | X-ray | 1.71 Å | A=1-363 |
| 5M5R | X-ray | 1.76 Å | A=1-363 |
| 5M61 | X-ray | 1.84 Å | A/B=1-363 |
| 5M5S | X-ray | 1.88 Å | A/B=1-363 |
| 5M5V | X-ray | 1.96 Å | A/B=1-363 |
| 5M5U | X-ray | 2.15 Å | A/B=1-363 |
| 3GC3 | X-ray | 2.2 Å | B=1-363 |
| 1UTC | X-ray | 2.3 Å | A/B=1-363 |
| 1B89 | X-ray | 2.6 Å | A=1074-1522 |
| 3GD1 | X-ray | 3.5 Å | I=1-363 |
| 3QIL | X-ray | 3.92 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1521-1624 |
| 6WCJ | EM | 6.3 Å | A/C/D/G/H/I/K/L/M=1-1675 |
| 1XI4 | EM | 7.9 Å | A/B/C/D/E/F/G/H/I=1-1630 |
| 3IYV | EM | 7.9 Å | A/B/C/D/E/F/G/H/I=1-1630 |
| 3LVG | X-ray | 7.94 Å | A/B/C=1074-1675 |
| 3LVH | X-ray | 9.0 Å | A/B/C=1074-1675 |
| 1XI5 | EM | 12.0 Å | A/B/C/D/E/F/G/H/I=1-1630 |
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