1ECY: Protease inhibitor ecotin

Protease inhibitor ecotin. Determined by X-ray diffraction at 2.19 Å resolution. Released 12 Feb 1997.

Method
X-ray diffraction
Resolution
2.19 Å
Organism
Escherichia coli
Chains
1
Atoms
1,569
Mol. weight
21.47 kDa
Ligands
GLC, BGC
Released
12 Feb 1997

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

Secondary structure: helices and β-sheets

1ECY contains 5 α-helices and 12 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, 12 β-strands

ElementResiduesLengthSheet
α-helix13-164
β-strand2011
β-strand23-2532
α-helix33-353
β-strand36-48133
β-strand5514
β-strand56-6382
β-strand70-7892
β-strand93-9863
β-strand9914
α-helix102-1054
β-strand106-10833
β-strand115-11842
β-strand12011
β-strand124-13183
α-helix1321
α-helix139-1413

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
EcotinAprotein142Escherichia coliP23827 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1ECY_1 ECOTIN (chains A)
AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLE
NKTLEGWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTP
DNVDVKYRVWKAEEKIDNAVVR

Ligands and cofactors

IDNameFormulaCopies
GLCalpha-D-glucopyranoseC6 H12 O64
BGCbeta-D-glucopyranoseC6 H12 O61

Primary citation

Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability. Shin, D.H., Song, H.K., Seong, I.S. et al. Protein Sci (1996) 5:2236-2247. PubMed

Other PDB entries of the same protein (UniProt P23827 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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