SAXSdb — 5cpa

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

CARBOXYPEPTIDASE A

Bos taurus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CBPA1_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–307； UniProt 111–417

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	5cpa
Deposition date deposition_date	1982-05-06
Structure title title	REFINED CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE A AT 1.54 ANGSTROMS RESOLUTION.
Keywords keywords	HYDROLASE (C-TERMINAL PEPTIDASE); HYDROLASE (C-TERMINAL PEPTIDASE)
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.

5cpa__assembly_1__model_1

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

Download this curve (.dat)

5cpa__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5cpa__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.38 Å
Rg (electron density)	18.02 Å
Total Rg	19.09 Å
Atom count	2438
Residues	307
Excluded volume	43217 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5cpa__assembly_1__model_1`	monomeric （1）	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 (3)

Entity 1 Entity 1 polymer

Description description	CARBOXYPEPTIDASE A
Molecular weight formula_weight	34442.5 kDa
EC 编号 ec_number	3.4.17.1
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2753

ARSTNTFNYATYHTLDEIYDFMDLLVAQHPELVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTENYGQNPSFTAILDSMDIFLEIVTNPNGFAFTHSENRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKYGSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTVNN

Source Source

Source organism organism	Bos taurus
Common name common_name	cattle
NCBI taxonomy ID ncbi_taxonomy_id	9913

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	315

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d5cpaa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamily	c.56.5 — Zn-dependent exopeptidases
Family Family family	c.56.5.1 — Pancreatic carboxypeptidases

CATH v4.4 (1 domains)

Domain ID domain_id	5cpaA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	10 — Zn peptidases

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7. Citations (9)

Refined crystal structure of carboxypeptidase A at 1.54 A resolution.

J.Mol.Biol. (1983)

PMID: 6887246 · DOI: 10.1016/S0022-2836(83)80024-2 PRIMARY

Crystallographic Studies on Apocarboxypeptidase a and the Complex with Glycyl-L-Tyrosine

Proc.Natl.Acad.Sci.USA (1983)

Binding of Ligands to the Active Site of Carboxypeptidase A

Proc.Natl.Acad.Sci.USA (1981)

Zinc Environment and Cis Peptide Bonds in Carboxypeptidase a at 1.75-Angstroms Resolution

Proc.Natl.Acad.Sci.USA (1981)

Carboxypeptidase a Mechanisms

Proc.Natl.Acad.Sci.USA (1980)

Untitled

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

Carboxypeptidase A,A Protein and an Enzyme

Adv.Protein Chem. (1971)

Structure and Mechanism in the Enzymatic Activity of Carboxypeptidase a and Relations to Chemical Sequence

Acc.Chem.Res. (1970)

;The Structure of Carboxypeptidase A, Vii.The 2.0-Angstroms Resolution Studies of the Enzyme and of its Complex with Glycyltyrosine,and Mechanistic Deductions ;

Brookhaven Symposia in Biology (1969)

Unit-cell length a length_a	51.600 Å
Unit-cell length b length_b	60.270 Å
Unit-cell length c length_c	47.250 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.27 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

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

Resolution resolution	1.540 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

REFINED CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE A AT 1.54 ANGSTROMS RESOLUTION.

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

CARBOXYPEPTIDASE 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

5cpa__assembly_1__model_1

5cpa__assembly_1__model_1 | I(q)

5cpa__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (9)

REFINED CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE A AT 1.54 ANGSTROMS RESOLUTION.

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

CARBOXYPEPTIDASE 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

5cpa__assembly_1__model_1

5cpa__assembly_1__model_1 | I(q)

5cpa__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (9)