1N8O: Complex between bovine chymotrypsin and ecotin

Crystal structure of a complex between bovine chymotrypsin and ecotin. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 Dec 2002.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: Bos taurus, Escherichia coli
Chains: 4
Atoms: 3,009
Mol. weight: 41.38 kDa
Released: 18 Dec 2002

Explore 1N8O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1N8O contains 14 α-helices and 33 β-strands across 3 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 B: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-34	5	3
β-strand	40-48	9	3
β-strand	51-54	4	3
α-helix	56-58	3
β-strand	65-68	4	3
β-strand	72	1	4
β-strand	81-90	10	3
β-strand	95	1	5
β-strand	100	1	5
β-strand	104-108	5	3
α-helix	111-114	4
α-helix	121	1
β-strand	122	1	2
α-helix	123-125	3
β-strand	135-140	6	2

Chain C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	154	1	4
β-strand	156-163	8	2
α-helix	165-172	8
α-helix	173-175	3
β-strand	180-184	5	2
β-strand	189	1	1
β-strand	198-203	6	2
β-strand	206-217	12	2
β-strand	225-230	6	2
α-helix	231-233	3
α-helix	235-244	10

Chain E: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	13-17	5
β-strand	18	1	6
β-strand	20-25	6	6
α-helix	27-29	3
α-helix	33-35	3
β-strand	36-48	13	7
β-strand	53-54	2	2
β-strand	55	1	8
β-strand	57-63	7	6
β-strand	70-76	7	6
β-strand	81-83	3	2
β-strand	93-98	6	7
β-strand	99	1	8
α-helix	102-105	4
β-strand	106-108	3	7
β-strand	115-120	6	6
β-strand	124-131	8	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chymotrypsin A, A chain	A	protein	13	Bos taurus	P00766 (AlphaFold model)
Chymotrypsin A, b chain	B	protein	131	Bos taurus	P00766 (AlphaFold model)
Chymotrypsin A, C chain	C	protein	97	Bos taurus	P00766 (AlphaFold model)
ecotin	E	protein	142	Escherichia coli	P23827 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1N8O_1 Chymotrypsin A, A chain (chains A)
CGVPAIQPVLSGL

Sequence of entity 2 (B), FASTA

>1N8O_2 Chymotrypsin A, b chain (chains B)
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGS
SSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTT
CVTTGWGLTRY

Sequence of entity 3 (C), FASTA

>1N8O_3 Chymotrypsin A, C chain (chains C)
ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWT
LVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN

Sequence of entity 4 (E), FASTA

>1N8O_4 ecotin (chains E)
AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLE
NKTLEGWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTP
DNVDVKYRVWKAEEKIDNAVVR

Primary citation

Crystal Structure of a Complex Between Bovine Chymotrypsin and Ecotin at 2.0 A Resolution. Cambillau, C., Spinelli, S., Lauwereys, M. To be published.

Other PDB entries of the same protein (UniProt P00766 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5R43 1.0 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 7.5, cryo temperature
5R42 1.05 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 7.5, room temperature
5R44 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 7.5, room temperature
5R45 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 7.5, cryo temperature
5R46 1.05 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, room temperature
5R48 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 5.6, room temperature
5R49 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 5.6, cryo temperature
5R4B 1.05 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 9, cryo temperature
5R4D 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 9, cryo temperature
5R47 1.1 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, cryo temperature
5R4C 1.15 Å, Crystal Structure of gamma-Chymotrypsin at pH 9, room temperature
5R4A 1.2 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 9, room temperature

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