SAXSdb — 1rg0

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

Fimbrial protein

Pseudomonas aeruginosa

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FMP1_PSEAE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–126； UniProt 36–157 Author chain B； PDBConstruct 5–126； UniProt 36–157

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	1rg0
Deposition date deposition_date	2003-11-10
Structure title title	Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa
Keywords keywords	Type IV Pilin, Lectin, Adhesin, Pseudomonas, CELL ADHESION; CELL ADHESION
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.

1rg0__assembly_1__model_1

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

Download this curve (.dat)

1rg0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1rg0__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.54 Å
Rg (electron density)	23.79 Å
Total Rg	24.40 Å
Atom count	1790
Residues	252
Excluded volume	31763 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1rg0__assembly_1__model_1`	dimeric （2）	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) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1rg0a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.24 — Pili subunits
Superfamily Superfamily superfamily	d.24.1 — Pili subunits
Family Family family	d.24.1.1 — Pilin

Domain ID domain_id	d1rg0a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1rg0b1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.24 — Pili subunits
Superfamily Superfamily superfamily	d.24.1 — Pili subunits
Family Family family	d.24.1.1 — Pilin

Domain ID domain_id	d1rg0b2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	1rg0A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	700 — Glycoprotein, Type 4 Pilin
Homologous superfamily homologous superfamily	10 — Glycoprotein, Type 4 Pilin

Domain ID domain_id	1rg0B00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	700 — Glycoprotein, Type 4 Pilin
Homologous superfamily homologous superfamily	10 — Glycoprotein, Type 4 Pilin

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Unit-cell length a length_a	37.301 Å
Unit-cell length b length_b	80.720 Å
Unit-cell length c length_c	39.127 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	113.37 °
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	1.800 Å
Low-resolution limit resolution_low	40.490 Å
R factor r_factor	0.2366
R_work r_work	0.2358
R_free r_free	0.2543

Description description	Fimbrial protein
Molecular weight formula_weight	12845.4 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	1887

Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa

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

Fimbrial protein

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

1rg0__assembly_1__model_1

1rg0__assembly_1__model_1 | I(q)

1rg0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

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) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

7. Citations (2)

Source organism organism	Pseudomonas aeruginosa
NCBI taxonomy ID ncbi_taxonomy_id	287
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	89

Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa

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

Fimbrial protein

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

1rg0__assembly_1__model_1

1rg0__assembly_1__model_1 | I(q)

1rg0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

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) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

7. Citations (2)