1EZU: Ecotin Y69F, D70P

Ecotin Y69F, D70P bound to D102N trypsin. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Jun 2000.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Escherichia coli, Rattus norvegicus
Chains: 4
Atoms: 5,554
Mol. weight: 79.88 kDa
Ligands: CA
Released: 23 Jun 2000

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

Secondary structure: helices and β-sheets

1EZU contains 32 α-helices and 68 β-strands across 4 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: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	7-9	3
α-helix	13-17	5
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	56-64	9	1
β-strand	69-83	15	1
α-helix	85-87	3
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	124-132	9	2
β-strand	137-138	2	2
β-strand	140-141	2	4

Chain B: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	204-206	3
α-helix	207-209	3
α-helix	213-217	5
β-strand	220-225	6	4
α-helix	227-229	3
α-helix	233-235	3
β-strand	236-248	13	2
β-strand	253-254	2	5
β-strand	255	1	6
β-strand	258-264	7	4
β-strand	269-275	7	4
β-strand	281-283	3	5
α-helix	285-287	3
β-strand	293-298	6	2
β-strand	299	1	6
α-helix	302-305	4
β-strand	306-308	3	2
β-strand	315-320	6	4
β-strand	324-338	15	2
β-strand	340-341	2	1

Chain C: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	417	1	7
β-strand	420-421	2	8
α-helix	422-423	2
β-strand	430-434	5	9
β-strand	440-448	9	9
β-strand	451-454	4	9
α-helix	456-458	3
β-strand	464-468	4	9
β-strand	472	1	10
β-strand	481-490	10	9
β-strand	495	1	11
β-strand	500	1	11
β-strand	504-508	5	9
β-strand	522	1	8
α-helix	523-524	2
α-helix	528-530	3
β-strand	535-540	6	8
β-strand	554	1	10
α-helix	555	1
β-strand	556-561	6	8
β-strand	562	1	5
α-helix	563-564	2
α-helix	565-571	7
β-strand	580-583	4	5
β-strand	589	1	7
β-strand	598-601	4	8
β-strand	604-612	5	8
β-strand	613-616	4	5
β-strand	626-629	4	5
α-helix	631-633	3
α-helix	635-644	10

Chain D: 9 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	717	1	12
β-strand	720-721	2	1
α-helix	722-723	2
β-strand	730-734	5	13
β-strand	740-748	9	13
β-strand	751-754	4	13
α-helix	756-758	3
β-strand	764-768	4	13
β-strand	772	1	14
β-strand	781-790	10	13
β-strand	795	1	15
β-strand	800	1	15
β-strand	804-808	5	13
β-strand	822	1	1
α-helix	823-824	2
α-helix	828-830	3
β-strand	835-840	6	1
β-strand	854	1	14
α-helix	855	1
β-strand	856-862	7	1
α-helix	863-864	2
α-helix	865-871	7
β-strand	880-883	4	1
β-strand	889	1	12
β-strand	898-901	4	1
β-strand	904-916	9	1
β-strand	926-930	5	1
α-helix	932-934	3
α-helix	935-944	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ecotin	A, B	protein	142	Escherichia coli	P23827 (AlphaFold model)
Trypsin II, anionic	C, D	protein	223	Rattus norvegicus	P00763 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1EZU_1 ECOTIN (chains A, B)
AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLE
NKTLEGWGFPYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTP
DNVDVKYRVWKAEEKIDNAVVR

Sequence of entity 2 (C, D), FASTA

>1EZU_2 TRYPSIN II, ANIONIC (chains C, D)
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEG
DEQFVNAAKIIKHPNFDRKTLNNNIMLIKLSSPVKLNARVATVALPSSCAPAGTQCLISG
WGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKDSCQGDSGGP
VVCNGELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2

Primary citation

Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases. Gillmor, S.A., Takeuchi, T., Yang, S.Q. et al. J Mol Biol (2000) 299:993-1003. DOI 10.1006/jmbi.2000.3812 · 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
7PQN 2.4 Å, Catalytic fragment of MASP-2 in complex with ecotin

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