Rac GTPase-activating protein 1 (RACGAP1) is a 632-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H0H5.
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The mean pLDDT of this model is 70.2 (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 | 36% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 33% |
What pLDDT means and how to read it
Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related…
Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex. Associates with alpha-, beta- and gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP domain and basic region with PRC1. The interaction with PRC1 inhibits its GAP activity towards CDC42 in vitro, which may be…
Nucleus, Cytoplasm, Cytoplasm, cytoskeleton, spindle, Cytoplasmic vesicle, secretory vesicle, acrosome, Cleavage furrow, Midbody, Midbody ring, Cell membrane, Midbody
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5C2K | X-ray | 1.42 Å | A=346-546 |
| 2OVJ | X-ray | 1.49 Å | A=348-546 |
| 3WPQ | X-ray | 1.84 Å | A/B=346-546 |
| 3W6R | X-ray | 1.9 Å | A=348-546 |
| 4B6D | X-ray | 2.2 Å | A/B/C/D/E/F=284-339 |
| 5C2J | X-ray | 2.5 Å | A=346-546 |
| 3WPS | X-ray | 2.7 Å | A/B=346-546 |
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