Kinesin-1 heavy chain (KIF5B) is a 963-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P33176.
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The mean pLDDT of this model is 78.6 (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 | 30% |
| 70 to 90 | Confident: backbone generally right | 51% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (By similarity). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes (PubMed:20386726). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). Through binding with PLEKHM2 and ARL8B, directs lysosome movement toward microtubule plus ends…
Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and PPP1R42 (By similarity). Interacts with SYBU (PubMed:15459722). Interacts with JAKMIP1 (PubMed:17532644). Interacts with PLEKHM2 (PubMed:15905402). Interacts with ECPAS (PubMed:20682791). Interacts with ZFYVE27 (By similarity). Found in a complex with OGT, RHOT1, RHOT2 and TRAK1 (PubMed:24995978). Interacts with…
Cytoplasm, cytoskeleton, Cytolytic granule membrane, Lysosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1BG2 | X-ray | 1.8 Å | A=1-325 |
| 5LT1 | X-ray | 1.95 Å | A/B=1-325 |
| 5LT0 | X-ray | 2.0 Å | A=1-325 |
| 4LNU | X-ray | 2.19 Å | K=1-325 |
| 9L7E | X-ray | 2.4 Å | A=1-349 |
| 5LT3 | X-ray | 2.59 Å | A/B/C/D/E/K=1-325 |
| 5LT2 | X-ray | 2.6 Å | A/B/C/D/E/K=1-325 |
| 1MKJ | X-ray | 2.7 Å | A=1-349 |
| 9L6K | X-ray | 2.8 Å | A/B=2-336 |
| 9L78 | X-ray | 2.82 Å | A/B=2-336 |
| 5LT4 | X-ray | 2.88 Å | A/B/C/D/E/K=1-325 |
| 9GNQ | EM | 2.9 Å | K=1-357 |
| 8RHB | EM | 3.0 Å | K/T/t=1-963 |
| 8RHH | EM | 3.0 Å | K/L/T/t=1-963 |
| 4HNA | X-ray | 3.19 Å | K=1-349 |
| 9L7M | EM | 3.48 Å | K=1-349 |
| 8RIK | EM | 3.6 Å | K/T/t=1-963 |
| 8RIZ | EM | 3.6 Å | K/L/T=1-963 |
| 6OJQ | EM | 3.67 Å | K=8-324 |
| 8IXA | EM | 4.2 Å | S/T/U/V/W/X/Y/Z/a=1-349 |
Showing 20 of 29 experimental structures (best resolution first).
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