5R42: Gamma-Chymotrypsin

Crystal Structure of deuterated gamma-Chymotrypsin at pH 7.5, room temperature. Determined by X-ray diffraction at 1.05 Å resolution. Released 1 Sept 2021.

Method: X-ray diffraction
Resolution: 1.05 Å
Organism: Bos taurus
Chains: 5
Atoms: 2,089
Mol. weight: 26.5 kDa
Released: 1 Sept 2021

Explore 5R42 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5R42 contains 8 α-helices and 24 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 B: 4 helices, 15 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
β-strand	115	1	6
β-strand	118	1	6
α-helix	120-121	2
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	156-162	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 D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	427-428	2	2

Chain E: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	225-227	3	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
gamma-Chymotrypsin	A	protein	13	Bos taurus	P00766 (AlphaFold model)
gamma-Chymotrypsin	B	protein	131	Bos taurus	P00766 (AlphaFold model)
gamma-Chymotrypsin	C	protein	97	Bos taurus	P00766 (AlphaFold model)
peptide SWPW	D	protein	4	Bos taurus
peptide TPGVY	E	protein	5	Bos taurus

Sequence of entity 1 (A), FASTA

>5R42_1 gamma-Chymotrypsin (chains A)
CGVPAIQPVLSGL

Sequence of entity 2 (B), FASTA

>5R42_2 gamma-Chymotrypsin (chains B)
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGS
SSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTT
CVTTGWGLTRY

Sequence of entity 3 (C), FASTA

>5R42_3 gamma-Chymotrypsin (chains C)
ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWT
LVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN

Sequence of entity 4 (D), FASTA

>5R42_4 peptide SWPW (chains D)
SWPW

Sequence of entity 5 (E), FASTA

>5R42_5 peptide TPGVY (chains E)
TPGVY

Primary citation

Effect of Temperature and pH on Ionizable Residues in gamma-Chymotrypsin: a X-ray and Neutron Crystallography Study. Kreinbring, C.A., Wilson, M.A., Kovalevsky, A.Y. et al. 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
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
1YPH 1.34 Å, High resolution structure of bovine alpha-chymotrypsin

Browse structure collections

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