Receptor-interacting serine/threonine-protein kinase 2 (RIPK2) is a 540-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43353.
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The mean pLDDT of this model is 76.1 (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 | 52% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 25% |
What pLDDT means and how to read it
Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and…
Interacts (via CARD domain) with NOD2 (via CARD domain) (PubMed:15044951, PubMed:17355968, PubMed:19592251, PubMed:21887730, PubMed:27812135, PubMed:30279485, PubMed:30478312). Interacts (via CARD domain) with NOD1 (via CARD domain) (PubMed:17054981, PubMed:30478312). Homooligomer; following interaction with NOD1 or NOD2, homooligomerizes via its CARD domain and forms long filaments named…
Cytoplasm, Cell membrane, Endoplasmic reticulum
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7OBS | X-ray | 1.8 Å | B=530-540 |
| 9F3V | X-ray | 1.94 Å | A/B=1-316 |
| 5NG0 | X-ray | 2.0 Å | A/B=1-300 |
| 8X2O | X-ray | 2.26 Å | A/B=1-316 |
| 7OBT | X-ray | 2.3 Å | B=530-540 |
| 6ES0 | X-ray | 2.38 Å | A/B=3-317 |
| 5AR2 | X-ray | 2.44 Å | A/B=1-310 |
| 5J7B | X-ray | 2.53 Å | A/B=1-310 |
| 6HMX | X-ray | 2.53 Å | A/B=1-310 |
| 6SZJ | X-ray | 2.53 Å | A/B=1-310 |
| 5NG3 | X-ray | 2.6 Å | A/B/C/D=1-300 |
| 6RNA | X-ray | 2.62 Å | A/B=1-310 |
| 5AR5 | X-ray | 2.66 Å | A/B=1-310 |
| 6UL8 | X-ray | 2.68 Å | A/B=5-310 |
| 5J79 | X-ray | 2.69 Å | A/B=1-310 |
| 6RN8 | X-ray | 2.69 Å | A/B=1-310 |
| 5AR4 | X-ray | 2.7 Å | A/B=1-310 |
| 5AR7 | X-ray | 2.71 Å | A/B=1-310 |
| 4C8B | X-ray | 2.75 Å | A/B=8-317 |
| 5AR8 | X-ray | 2.79 Å | A/B=1-310 |
Showing 20 of 33 experimental structures (best resolution first).
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