1ECZ: Protease inhibitor ecotin

Name: PDB 1ECZ: Protease inhibitor ecotin
Published: 1997-02-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: protease inhibitor

Protease inhibitor ecotin. Determined by X-ray diffraction at 2.68 Å resolution. Released 12 Feb 1997.

Method: X-ray diffraction
Resolution: 2.68 Å
Organism: Escherichia coli
Chains: 2
Atoms: 2,767
Mol. weight: 38.38 kDa
Ligands: BOG
Released: 12 Feb 1997

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

Secondary structure: helices and β-sheets

1ECZ contains 7 α-helices and 34 β-strands across 2 chains. 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: 3 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	7-9	3
α-helix	13-16	4
β-strand	20	1	1
β-strand	23-26	4	2
α-helix	27-29	3
β-strand	36-41	6	3
β-strand	43-48	6	4
β-strand	53-54	2	5
β-strand	55	1	6
β-strand	58-64	7	2
β-strand	69-75	7	2
β-strand	81-82	2	5
β-strand	93-98	6	4
β-strand	99	1	6
β-strand	106-108	3	3
β-strand	114-118	5	2
β-strand	120	1	1
β-strand	126-132	7	3
β-strand	137-138	2	3
β-strand	140	1	7

Chain B: 4 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	7-9	3
β-strand	20	1	8
β-strand	23-25	3	7
α-helix	27-29	3
β-strand	36-41	6	3
β-strand	43-48	6	9
β-strand	53-54	2	10
β-strand	55	1	11
β-strand	59-64	6	7
β-strand	69-74	6	7
α-helix	78-80	3
β-strand	81-82	2	10
β-strand	93-98	6	9
β-strand	99	1	11
α-helix	102-105	4
β-strand	108	1	3
β-strand	115-118	4	7
β-strand	120	1	8
β-strand	126-131	6	3
β-strand	137-138	2	3
β-strand	140	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ecotin	A, B	protein	142	Escherichia coli	P23827 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1ECZ_1 ECOTIN (chains A, B)
AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLE
NKTLEGWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTP
DNVDVKYRVWKAEEKIDNAVVR

Ligands and cofactors

ID	Name	Formula	Copies
BOG	octyl beta-D-glucopyranoside	C14 H28 O6	21

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:

1SLU 1.8 Å, Rat anionic N143H, E151H trypsin complexed to A86H ecotin
1IFG 2.0 Å, Crystal structure of a monomeric form of general protease inhibitor, ecotin in absence…
1N8O 2.0 Å, Crystal structure of a complex between bovine chymotrypsin and ecotin
1SLW 2.0 Å, Rat anionic N143H, E151H trypsin complexed to A86H ecotin; nickel-bound
1ECY 2.19 Å, Protease inhibitor ecotin
1FI8 2.2 Å, Rat granzyme B [N66Q] complexed to ecotin [81-84 iepd]
1SLX 2.2 Å, Rat anionic N143H, E151H trypsin complexed to A86H ecotin; zinc-bound
1XX9 2.2 Å, Crystal Structure of the FXIa Catalytic Domain in Complex with EcotinM84R
1AZZ 2.3 Å, Fiddler crab collagenase complexed to ecotin
1EZS 2.3 Å, Crystal structure of ecotin mutant M84R, W67A, G68A, Y69A, D70A bound to rat anionic…
1SLV 2.3 Å, Rat anionic N143H, E151H trypsin complexed to A86H ecotin; copper-bound
1EZU 2.4 Å, Ecotin Y69F, D70P bound to D102N trypsin

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