1GG6: Gamma chymotrypsin

Crystal structure of gamma chymotrypsin with N-acetyl-phenylalanine trifluoromethyl ketone bound at the active site. Determined by X-ray diffraction at 1.4 Å resolution. Released 20 Sept 2000.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: Bos taurus
Chains: 3
Atoms: 2,161
Mol. weight: 26.08 kDa
Ligands: APL, APF
Released: 20 Sept 2000

Explore 1GG6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GG6 contains 7 α-helices and 22 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 B: 3 helices, 14 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
β-strand	135-140	6	2
β-strand	145	1	6

Chain C: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	150	1	6
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	206-215	10	2
β-strand	225-230	6	2
α-helix	231-233	3
α-helix	235-244	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Gamma chymotrypsin	A	protein	10	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)

Sequence of entity 1 (A), FASTA

>1GG6_1 GAMMA CHYMOTRYPSIN (chains A)
CGVPAIQPVL

Sequence of entity 2 (B), FASTA

>1GG6_2 GAMMA CHYMOTRYPSIN (chains B)
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGS
SSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTT
CVTTGWGLTRY

Sequence of entity 3 (C), FASTA

>1GG6_3 GAMMA CHYMOTRYPSIN (chains C)
ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWT
LVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN

Ligands and cofactors

ID	Name	Formula	Copies
APL	N-(1-benzyl-3,3,3-trifluoro-2,2-dihydroxy-propyl)-acetamide	C12 H14 F3 N O3	1
APF	1,1,1-trifluoro-3-acetamido-4-phenyl butan-2-one(n-acetyl-L-phenylalanyl…	C12 H12 F3 N O2	1

Water and common crystallization additives (SO4, EDO) are not listed.

Primary citation

Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin. Neidhart, D., Wei, Y., Cassidy, C. et al. Biochemistry (2001) 40:2439-2447. DOI 10.1021/bi002535a · 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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