1ACB: Alpha-chymotrypsin

Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin C complex at 2.0 Å resolution. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Oct 1993.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: Bos taurus, Hirudo medicinalis
Chains: 2
Atoms: 2,431
Mol. weight: 33.79 kDa
Released: 31 Oct 1993

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

Secondary structure: helices and β-sheets

1ACB contains 11 α-helices and 31 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 E: 9 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	7-8	2
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-34	5	3
β-strand	40-46	7	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
β-strand	115	1	6
β-strand	118	1	6
α-helix	120-121	2
β-strand	122	1	2
α-helix	123-124	2
β-strand	135-140	6	2
β-strand	145	1	7
β-strand	150	1	7
β-strand	154	1	4
β-strand	156-162	7	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 I: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	9	1	8
α-helix	11-13	3
β-strand	17	1	8
α-helix	18-28	11
β-strand	33-38	6	8
β-strand	42-44	3	2
β-strand	51-57	7	8
β-strand	62-63	2	8
β-strand	68-69	2	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-chymotrypsin	E	protein	245	Bos taurus	P00766 (AlphaFold model)
Eglin C	I	protein	70	Hirudo medicinalis	P01051 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>1ACB_1 ALPHA-CHYMOTRYPSIN (chains E)
CGVPAIQPVLSGLSRIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGV
TTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSA
VCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAM
ICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQ
TLAAN

Sequence of entity 2 (I), FASTA

>1ACB_2 Eglin C (chains I)
TEFGSELKSFPEVVGKTVDQAREYFTLHYPQYDVYFLPEGSPVTLDLRYNRVRVFYNPGT
NVVNHVPHVG

Primary citation

Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution. Frigerio, F., Coda, A., Pugliese, L. et al. J Mol Biol (1992) 225:107-123. DOI 10.1016/0022-2836(92)91029-O · PubMed

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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