SAXSdb — 1col

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

COLICIN A

Escherichia coli

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CEA_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–204； UniProt 389–592 Author chain B； PDBConstruct 1–204； UniProt 389–592

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	1col
Deposition date deposition_date	1991-07-06
Structure title title	REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION
Keywords keywords	ANTIBACTERIAL PROTEIN; ANTIBACTERIAL PROTEIN
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.

1col__assembly_1__model_1

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

Download this curve (.dat)

1col__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1col__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.93 Å
Rg (electron density)	15.44 Å
Total Rg	16.62 Å
Atom count	1478
Residues	197
Excluded volume	26615 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1col__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1col__assembly_2__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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1cola_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.1 — Toxins' membrane translocation domains
Superfamily Superfamily superfamily	f.1.1 — Colicin
Family Family family	f.1.1.1 — Colicin

Domain ID domain_id	d1colb_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.1 — Toxins' membrane translocation domains
Superfamily Superfamily superfamily	f.1.1 — Colicin
Family Family family	f.1.1.1 — Colicin

CATH v4.4 (2 domains)

Domain ID domain_id	1colA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	490 — Globin-like
Homologous superfamily homologous superfamily	30 — Colicin

Domain ID domain_id	1colB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	490 — Globin-like
Homologous superfamily homologous superfamily	30 — Colicin

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7. Citations (7)

Refined structure of the pore-forming domain of colicin A at 2.4 A resolution.

J.Mol.Biol. (1992)

PMID: 1373773 · DOI: 10.1016/0022-2836(92)90550-4 PRIMARY

Fluorescence Energy Transfer Distance Measurements Using Site-Directed Single Cysteine Mutants

J.Mol.Biol. (1991)

Colicins: Prokaryotic Killer-Pores

Experientia (1990)

Structure of the Membrane-Pore-Forming Fragment of Colicin A

Nature (1989)

The Membrane Channel-Forming Colicin A: Synthesis, Secretion, Structure, Action and Immunity

Biochim.Biophys.Acta (1988)

Gating Processes of Channels Induced by Colicin A, its C-Terminal Fragment and Colicin E1 in Planar Lipid Bilayers

Eur.Biophys.J. (1987)

Crystallization of the C-Terminal Domain of Colicin A Carrying the Voltage-Dependent Pore Activity of the Protein

J.Mol.Biol. (1986)

Unit-cell length a length_a	73.000 Å
Unit-cell length b length_b	73.000 Å
Unit-cell length c length_c	171.600 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	16

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	0.1800
R_work r_work	—
R_free r_free	—

Description description	COLICIN A
Molecular weight formula_weight	21818.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3039

REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION

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

COLICIN 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

1col__assembly_1__model_1

1col__assembly_1__model_1 | I(q)

1col__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (7)

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	83

REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION

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

COLICIN 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

1col__assembly_1__model_1

1col__assembly_1__model_1 | I(q)

1col__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (7)