1IFG: Ecotin

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.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Escherichia coli
Chains
1
Atoms
1,167
Mol. weight
15.85 kDa
Released
18 May 2001

Explore 1IFG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 5 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix7-93
α-helix13-164
β-strand20-2561
α-helix27-293
α-helix33-353
β-strand36-48132
β-strand53-5421
β-strand5513
β-strand56-6381
β-strand70-82131
β-strand93-9862
β-strand9913
α-helix102-1054
β-strand106-10832
β-strand115-12061
β-strand124-130A82
β-strand131-13222
β-strand137-13822
β-strand140-14121

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
EcotinAprotein140Escherichia coliP23827 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1IFG_1 ECOTIN (chains A)
PLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLENKTLE
GWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTPDNVDV
KYRVWADGKAEEKIDNAVVR

Primary citation

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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