1GCT: Gamma-chymotrypsin a

Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of gamma-chymotrypsin? Determined by X-ray diffraction at 1.6 Å resolution. Released 15 Oct 1991.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Bos taurus
Chains: 4
Atoms: 1,935
Mol. weight: 25.85 kDa
Released: 15 Oct 1991

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

Secondary structure: helices and β-sheets

1GCT contains 8 α-helices and 21 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: 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	40-48	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	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	206-216	11	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	502-503	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Gamma-chymotrypsin a	A	protein	13	Bos taurus	P00766 (AlphaFold model)
Gamma-chymotrypsin a	B	protein	131	Bos taurus	P00766 (AlphaFold model)
Gamma-chymotrypsin a	C	protein	97	Bos taurus	P00766 (AlphaFold model)
Tetrapeptide adduct	D	protein	5

Sequence of entity 1 (A), FASTA

>1GCT_1 GAMMA-CHYMOTRYPSIN A (chains A)
CGVPAIQPVLSGL

Sequence of entity 2 (B), FASTA

>1GCT_2 GAMMA-CHYMOTRYPSIN A (chains B)
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGS
SSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTT
CVTTGWGLTRY

Sequence of entity 3 (C), FASTA

>1GCT_3 GAMMA-CHYMOTRYPSIN A (chains C)
ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWT
LVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN

Sequence of entity 4 (D), FASTA

>1GCT_4 TETRAPEPTIDE ADDUCT (chains D)
XPGAY

Primary citation

Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin? Dixon, M.M., Matthews, B.W. Biochemistry (1989) 28:7033-7038. DOI 10.1021/bi00443a038 · 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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