SAXSdb — 2gch

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1. Protein Identity and Related Structures Protein Identity & Related Structures

GAMMA-CHYMOTRYPSIN A

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 6	water × 6	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 3	water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CTRA_BOVIN
Isoform	—
PDB entities	1, 2, 3
Chains and sequence ranges	Author chain E； PDBConstruct 1–13； UniProt 1–13 Author chain F； PDBConstruct 1–131； UniProt 16–146 Author chain G； PDBConstruct 1–97； UniProt 149–245

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2gch
Deposition date deposition_date	1980-05-21
Structure title title	REFINED CRYSTAL STRUCTURE OF GAMMA-CHYMOTRYPSIN AT 1.9 ANGSTROMS RESOLUTION
Keywords keywords	HYDROLASE (SERINE PROTEINASE); HYDROLASE (SERINE PROTEINASE)
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2gch__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2gch__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2gch__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	23.21 Å
Rg (electron density)	22.29 Å
Total Rg	23.15 Å
Atom count	3476
Residues	474
Excluded volume	61930 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2gch__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2gch__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	GAMMA-CHYMOTRYPSIN A
Molecular weight formula_weight	1253.5 kDa
EC 编号 ec_number	3.4.21.1
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E
Atom count atom_count	1889

CGVPAIQPVLSGL

Entity 2 Entity 2 polymer

Description description	GAMMA-CHYMOTRYPSIN A
Molecular weight formula_weight	13934.6 kDa
EC 编号 ec_number	3.4.21.1
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F

IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRY

Entity 3 Entity 3 polymer

Description description	GAMMA-CHYMOTRYPSIN A
Molecular weight formula_weight	10074.5 kDa
EC 编号 ec_number	3.4.21.1
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	151

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2gch.1
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.2 — Eukaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id	2gchF00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	2gchG00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

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7. Citations (9)

Refined crystal structure of gamma-chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases.

J.Mol.Biol. (1981)

PMID: 6914398 · DOI: 10.1016/0022-2836(81)90186-8 PRIMARY

Untitled

Atlas of Macromolecular Structure on Microfiche (1976)

The Stereochemistry of Substrate Binding to Chymotrypsin A Gamma

Cold Spring Harbor Symp.Quant.Biol. (1972)

Untitled

Atlas of Protein Sequence and Structure (Data Section) (1972)

;Substrate Binding Site in Chymotrypsin A Gamma, Crystallographic Study Using Peptide Chloromethyl Ketones as Site-Specific Inhibitors ;

Biochemistry (1971)

The Relation between Gamma-and Alpha-Chymotrypsin, II.Direct Comparison of the Electron Densities at 5.5 Angstroms Resolution

Acta Crystallogr.,Sect.B (1970)

Structure of Gamma-Chymotrypsin at 5.5 Angstroms Resolution

J.Mol.Biol. (1969)

Relation between Gamma-and Alpha-Chymotrypsin

J.Mol.Biol. (1968)

The Isomorphous Heavy-Atom Substitution at the Active Site of Gamma Chymotrypsin

Proc.Natl.Acad.Sci.USA (1964)

Unit-cell length a length_a	69.600 Å
Unit-cell length b length_b	69.600 Å
Unit-cell length c length_c	97.400 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 42 21 2
Space-group number int_tables_number	94
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	7.000 Å
R factor r_factor	—
R_work r_work	0.1810
R_free r_free	—

REFINED CRYSTAL STRUCTURE OF GAMMA-CHYMOTRYPSIN AT 1.9 ANGSTROMS RESOLUTION

1. Protein Identity and Related Structures Protein Identity & Related Structures

GAMMA-CHYMOTRYPSIN A

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2gch__assembly_1__model_1

2gch__assembly_1__model_1 | I(q)

2gch__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (9)

REFINED CRYSTAL STRUCTURE OF GAMMA-CHYMOTRYPSIN AT 1.9 ANGSTROMS RESOLUTION

1. Protein Identity and Related Structures Protein Identity & Related Structures

GAMMA-CHYMOTRYPSIN A

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2gch__assembly_1__model_1

2gch__assembly_1__model_1 | I(q)

2gch__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (9)