Crystal structure of a monomeric form of general protease inhibitor, ecotin in absence of a protease. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 May 2001.
Explore 1IFG in 3D Show helices and sheets RCSB PDB PDBe
1IFG contains 5 α-helices and 14 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-9 | 3 | |
| α-helix | 13-16 | 4 | |
| β-strand | 20-25 | 6 | 1 |
| α-helix | 27-29 | 3 | |
| α-helix | 33-35 | 3 | |
| β-strand | 36-48 | 13 | 2 |
| β-strand | 53-54 | 2 | 1 |
| β-strand | 55 | 1 | 3 |
| β-strand | 56-63 | 8 | 1 |
| β-strand | 70-82 | 13 | 1 |
| β-strand | 93-98 | 6 | 2 |
| β-strand | 99 | 1 | 3 |
| α-helix | 102-105 | 4 | |
| β-strand | 106-108 | 3 | 2 |
| β-strand | 115-120 | 6 | 1 |
| β-strand | 124-130A | 8 | 2 |
| β-strand | 131-132 | 2 | 2 |
| β-strand | 137-138 | 2 | 2 |
| β-strand | 140-141 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ecotin | A | protein | 140 | Escherichia coli | P23827 (AlphaFold model) |
>1IFG_1 ECOTIN (chains A) PLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLENKTLE GWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTPDNVDV KYRVWADGKAEEKIDNAVVR
The role of ecotin dimerization in protease inhibition. Eggers, C.T., Wang, S.X., Fletterick, R.J. et al. J Mol Biol (2001) 308:975-991. DOI 10.1006/jmbi.2001.4754 · PubMed
Other PDB entries of the same protein (UniProt P23827 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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