Enoyl-[acyl-carrier-protein] reductase [NADH] (inhA) is a 269-residue protein from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P9WGR1.
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The mean pLDDT of this model is 94.2 (very high 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 | 84% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Enoyl-ACP reductase of the type II fatty acid syntase (FAS-II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls (PubMed:25227413). Catalyzes the NADH-dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway (PubMed:7599116). Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates (PubMed:7599116). The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain…
Homodimer (PubMed:7599116). Homotetramer (PubMed:10336454, PubMed:16647717)
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4TRO | X-ray | 1.4 Å | A=1-269 |
| 5G0T | X-ray | 1.54 Å | A/B/C/D=1-269 |
| 4OHU | X-ray | 1.6 Å | A/B/C/D=1-269 |
| 8OTM | X-ray | 1.6 Å | A/B/C/D=1-269 |
| 4TZK | X-ray | 1.62 Å | A=1-269 |
| 4U0J | X-ray | 1.62 Å | A=1-269 |
| 4D0S | X-ray | 1.64 Å | A/B/C/D=1-269 |
| 9RJK | X-ray | 1.66 Å | A/B/C/D=1-269 |
| 9RJL | X-ray | 1.7 Å | A/B/C/D/E/F=1-269 |
| 5OIP | X-ray | 1.71 Å | A=3-269 |
| 9RJG | X-ray | 1.71 Å | A/B/C/D/E/F=1-269 |
| 9RJH | X-ray | 1.71 Å | A/B/C/D/E/F=1-269 |
| 6SQD | X-ray | 1.72 Å | A=1-269 |
| 4TRJ | X-ray | 1.73 Å | A=1-269 |
| 4UVI | X-ray | 1.73 Å | A/B/C/D=1-269 |
| 5G0U | X-ray | 1.73 Å | A/B/C/D=1-269 |
| 5G0S | X-ray | 1.74 Å | A/B/C/D=1-269 |
| 6R9W | X-ray | 1.75 Å | A/B/C/D/E/F=1-269 |
| 6SQ9 | X-ray | 1.75 Å | A=1-269 |
| 6SQ7 | X-ray | 1.76 Å | A=1-269 |
Showing 20 of 126 experimental structures (best resolution first).
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