SAXSdb — 1o9w

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

F17A-G FIMBRIAL ADHESIN

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	2-acetamido-2-deoxy-beta-D-glucopyranose × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	F17AG_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–177； UniProt 23–199

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	1o9w
Deposition date deposition_date	2002-12-20
Structure title title	F17-aG lectin domain from Escherichia coli in complex with N-acetyl-glucosamine
Keywords keywords	BACTERIAL ADHESIN, BACTERIAL ATTACHMENT, SUGAR BINDING PROTEIN PATHOGENESIS, IMMUNOGLOBULIN FOLD, SUGAR BINDING PROTEIN; SUGAR BINDING 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.

1o9w__assembly_1__model_1

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

Download this curve (.dat)

1o9w__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1o9w__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.50 Å
Rg (electron density)	16.70 Å
Total Rg	17.59 Å
Atom count	1259
Residues	169
Excluded volume	22238 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1o9w__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	F17A-G FIMBRIAL ADHESIN
Molecular weight formula_weight	19048.2 kDa
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	1370

AVSFIGSTENDVGPSLGSYSRTHAMDNLPFVYDTRNKIGYQNANVWHISKGFCVGLDGKVDLPVVGSLDGQSIYGLTEEVGLLIWMGDTKYSRGTAMSGNSWENVFSGWCVGANTASTQGLSVRVTPVILKRNSSARYSVQKTSIGSIRMRPYNGSSAGSVQTTVNFSLNPFTLNDT

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
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	111

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1o9wa_
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.3 — Bacterial adhesins
Family Family family	b.2.3.5 — F17c-type adhesin

CATH v4.4 (1 domains)

Domain ID domain_id	1o9wA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1410 — Bacterial adhesins - F17c-type

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Unit-cell length a length_a	42.329 Å
Unit-cell length b length_b	42.329 Å
Unit-cell length c length_c	268.714 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 61 2 2
Space-group number int_tables_number	178
Crystal system crystal_system	—

Resolution resolution	1.650 Å
Low-resolution limit resolution_low	24.770 Å
R factor r_factor	0.2110
R_work r_work	0.2110
R_free r_free	0.2420

F17-aG lectin domain from Escherichia coli in complex with N-acetyl-glucosamine

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

F17A-G FIMBRIAL ADHESIN

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

1o9w__assembly_1__model_1

1o9w__assembly_1__model_1 | I(q)

1o9w__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 (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 (3)

F17-aG lectin domain from Escherichia coli in complex with N-acetyl-glucosamine

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

F17A-G FIMBRIAL ADHESIN

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

1o9w__assembly_1__model_1

1o9w__assembly_1__model_1 | I(q)

1o9w__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 (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 (3)