Nitric oxide synthase, inducible (Nos2) is a 1144-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P29477.
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The mean pLDDT of this model is 84.7 (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 | 61% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body (PubMed:7503239). In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (PubMed:16373578). As component of the iNOS-S100A8/9 transnitrosylase complex is involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (By similarity). Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8…
Homodimer (PubMed:10769116, PubMed:11669619). Interacts with NHERF1 (By similarity). Interacts with GAPDH (By similarity). Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9 transnitrosylase complex (By similarity). Interacts with SPSB1, SPSB2 and SPSB4 (PubMed:20603330). Interacts with ELOC and CUL5 in the presence of SPSB1 or SPSB2 or SPSB4 (By similarity). Forms a complex with ASL,…
Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3GOF | X-ray | 1.45 Å | C/D=503-518 |
| 2ORT | X-ray | 1.87 Å | A=114-498 |
| 2ORP | X-ray | 1.97 Å | A=114-498 |
| 2ORO | X-ray | 2.0 Å | A=114-498 |
| 2ORR | X-ray | 2.0 Å | A=114-498 |
| 2ORS | X-ray | 2.0 Å | A=114-498 |
| 3E7M | X-ray | 2.0 Å | A/B=66-498 |
| 3E65 | X-ray | 2.05 Å | A/B=66-498 |
| 1NOS | X-ray | 2.1 Å | A=115-498 |
| 2ORQ | X-ray | 2.1 Å | A=114-498 |
| 3E68 | X-ray | 2.2 Å | A/B=66-498 |
| 3EAI | X-ray | 2.2 Å | A/B=66-498 |
| 3NQS | X-ray | 2.2 Å | A/B=66-498 |
| 1DD7 | X-ray | 2.25 Å | A=114-498 |
| 3EBF | X-ray | 2.29 Å | A/B=66-498 |
| 1JWK | X-ray | 2.3 Å | A/B=66-498 |
| 1R35 | X-ray | 2.3 Å | A/B=66-498 |
| 2NOS | X-ray | 2.3 Å | A=115-498 |
| 3E6L | X-ray | 2.3 Å | A/B=66-498 |
| 1DF1 | X-ray | 2.35 Å | A/B=77-499 |
Showing 20 of 51 experimental structures (best resolution first).
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