SAXSdb — 4cha

▼

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

ALPHA-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 × 5	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 A； PDBConstruct 1–13； UniProt 1–13 Author chain E； PDBConstruct 1–13； UniProt 1–13 Author chain B； PDBConstruct 1–131； UniProt 16–146 Author chain F； PDBConstruct 1–131； UniProt 16–146 Author chain C； PDBConstruct 1–97； UniProt 149–245 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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	4cha
Deposition date deposition_date	1984-11-26
Structure title title	STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION
Keywords keywords	HYDROLASE (SERINE PROTEINASE); HYDROLASE (SERINE PROTEINASE)
Experimental Method method	X-RAY DIFFRACTION

▼

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.

4cha__assembly_1__model_1

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

Download this curve (.dat)

4cha__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4cha__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.02 Å
Rg (electron density)	22.29 Å
Total Rg	23.18 Å
Atom count	3506
Residues	477
Excluded volume	62424 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4cha__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	ALPHA-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	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,E
Atom count atom_count	3591

CGVPAIQPVLSGL

Entity 2 Entity 2 polymer

Description description	ALPHA-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	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,F

IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRY

Entity 3 Entity 3 polymer

Description description	ALPHA-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	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,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	85

▼

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d4cha.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

Domain ID domain_id	d4cha.2
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 (4 domains)

Domain ID domain_id	4chaB00
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	4chaC00
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	4chaF00
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	4chaG00
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

▶

7. Citations (15)

Structure of alpha-chymotrypsin refined at 1.68 A resolution.

J.Mol.Biol. (1985)

PMID: 4046030 · DOI: 10.1016/0022-2836(85)90314-6 PRIMARY

Structure and Mechanism of Chymotrypsin

Acc.Chem.Res. (1976)

The Active Centers of Serine Proteinases

Ann.N.Y.Acad.Sci. (1974)

Comparison of the Crystal Structures of Chymotrypsinogen-A and Alpha-Chymotrypsin

J.Mol.Biol. (1973)

Structure of Crystalline Alpha-Chymotrypsin. V. The Atomic Structure of Tosyl-Alpha-Chymotrypsin at 2 Angstroms Resolution

J.Mol.Biol. (1972)

Structure of Crystalline Methyl-Chymotrypsin

J.Mol.Biol. (1972)

Alpha-Chymotrypsin,What Can We Learn About Catalysis from X-Ray Diffraction (Query).

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

Chymotrypsin-Chemical Properties and Catalysis

The Enzymes,Third Edition (1971)

The Structure of Chymotrypsin

The Enzymes,Third Edition (1971)

The Structure of Alpha-Chymotrypsin

Philos.Trans.R.Soc.London,Ser.B (1970)

;Structure of Crystalline Alpha-Chymotrypsin. Iv. The Structure of Indoleacryloyl-Alpha-Chymotrypsin and its Relevance to the Hydrolytic Mechanism of the Enzyme ;

J.Mol.Biol. (1970)

The Study of Alpha-Chymotrypsin by X-Ray Diffraction

Biochem.J. (1969)

;Structure of Crystalline Alpha-Chymotrypsin. III. Crystallographic Studies of Substrates and Inhibitors Bound to the Active Site of Alpha-Chymotrypsin ;

J.Mol.Biol. (1969)

Structure of Crystalline Alpha-Chymotrypsin. II. A Preliminary Report Including a Hypothesis for the Activation Mechanism

J.Mol.Biol. (1968)

Three-Dimensional Structure of Tosyl-Alpha-Chymotrypsin

Nature (1967)

Unit-cell length a length_a	49.230 Å
Unit-cell length b length_b	67.390 Å
Unit-cell length c length_c	65.990 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	101.80 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.680 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION

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

ALPHA-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

4cha__assembly_1__model_1

4cha__assembly_1__model_1 | I(q)

4cha__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) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (15)

STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION

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

ALPHA-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

4cha__assembly_1__model_1

4cha__assembly_1__model_1 | I(q)

4cha__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) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (15)