1CHO: Alpha-chymotrypsin a

Crystal and molecular structures of the complex of alpha-*chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 Å resolution. Determined by X-ray diffraction at 1.8 Å resolution. Released 16 Jul 1988.

Method: X-ray diffraction
Resolution: 1.8 Å
Organisms: Bos taurus, Meleagris gallopavo
Chains: 4
Atoms: 2,371
Mol. weight: 31.29 kDa
Released: 16 Jul 1988

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

Secondary structure: helices and β-sheets

1CHO contains 8 α-helices and 24 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 F: 4 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	40-46	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
α-helix	120-121	2
β-strand	122	1	2
α-helix	123-125	3
β-strand	135-140	6	2

Chain G: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
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	231-244	14

Chain I: 1 helix, 4 β-strands

Element	Residues	Length	Sheet
β-strand	15-17	3	2
β-strand	23-25	3	6
β-strand	30-31	2	6
α-helix	34-43	10
β-strand	50-53	4	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-chymotrypsin a	E	protein	13	Bos taurus	P00766 (AlphaFold model)
Alpha-chymotrypsin a	F	protein	131	Bos taurus	P00766 (AlphaFold model)
Alpha-chymotrypsin a	G	protein	97	Bos taurus	P00766 (AlphaFold model)
Turkey ovomucoid third domain (OMTKY3)	I	protein	56	Meleagris gallopavo	P68390 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>1CHO_1 ALPHA-CHYMOTRYPSIN A (chains E)
CGVPAIQPVLSGL

Sequence of entity 2 (F), FASTA

>1CHO_2 ALPHA-CHYMOTRYPSIN A (chains F)
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGS
SSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTT
CVTTGWGLTRY

Sequence of entity 3 (G), FASTA

>1CHO_3 ALPHA-CHYMOTRYPSIN A (chains G)
ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWT
LVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN

Sequence of entity 4 (I), FASTA

>1CHO_4 TURKEY OVOMUCOID THIRD DOMAIN (OMTKY3) (chains I)
LAAVSVDCSEYPKPACTLEYRPLCGSDNKTYGNKCNFCNAVVESNGTLTLSHFGKC

Primary citation

Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution. Fujinaga, M., Sielecki, A.R., Read, R.J. et al. J Mol Biol (1987) 195:397-418. DOI 10.1016/0022-2836(87)90659-0 · 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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