SAXSdb — 2f1v

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

Outer membrane protein W

Escherichia coli K12

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	GLYCEROL × 1	Consistent with protein count
10	Protein homooligomer	Homooligomer	Protein 2	GLYCEROL × 2	Consistent with protein count
11	Protein homooligomer	Homooligomer	Protein 2	GLYCEROL × 2	Consistent with protein count
12	Protein homooligomer	Homooligomer	Protein 2	GLYCEROL × 2	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	GLYCEROL × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	GLYCEROL × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	GLYCEROL × 1	Consistent with protein count
5	Protein monomer	Monomer	Protein 1	GLYCEROL × 1	Consistent with protein count
6	Protein monomer	Monomer	Protein 1	GLYCEROL × 1	Consistent with protein count
7	Protein homooligomer	Homooligomer	Protein 6	GLYCEROL × 6	Consistent with protein count
8	Protein homooligomer	Homooligomer	Protein 3	GLYCEROL × 3	Consistent with protein count
9	Protein homooligomer	Homooligomer	Protein 3	GLYCEROL × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	OMPW_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–191； UniProt 22–212 Author chain B； PDBConstruct 1–191； UniProt 22–212 Author chain C； PDBConstruct 1–191； UniProt 22–212 Author chain D； PDBConstruct 1–191； UniProt 22–212 Author chain E； PDBConstruct 1–191； UniProt 22–212 Author chain F； PDBConstruct 1–191； UniProt 22–212

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	2f1v
Deposition date deposition_date	2005-11-15
Structure title title	Outer membrane protein OmpW
Keywords keywords	outer membrane protein beta barrel, MEMBRANE PROTEIN; MEMBRANE 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.

2f1v__assembly_10__model_1

Assembly 10 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2f1v__assembly_10__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2f1v__assembly_10__model_1 | P(r) · Pending

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

Rg（Guinier）	23.90 Å
Rg (electron density)	22.85 Å
Total Rg	23.60 Å
Atom count	2860
Residues	364
Excluded volume	50298 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2f1v__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2f1v__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2f1v__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2f1v__assembly_4__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`2f1v__assembly_5__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`2f1v__assembly_6__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`2f1v__assembly_7__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`2f1v__assembly_8__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
9	1	`2f1v__assembly_9__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
10	1	`2f1v__assembly_10__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
11	1	`2f1v__assembly_11__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
12	1	`2f1v__assembly_12__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

CATH v4.4 (6 domains)

Domain ID domain_id	2f1vA00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2f1vB00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2f1vC00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2f1vD00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2f1vE00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2f1vF00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	160 — Porin
Homologous superfamily homologous superfamily	20 —

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Unit-cell length a length_a	118.666 Å
Unit-cell length b length_b	118.776 Å
Unit-cell length c length_c	118.519 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	24

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2930
R_work r_work	0.2920
R_free r_free	0.3140

Description description	Outer membrane protein W
Molecular weight formula_weight	21700.1 kDa
Source method src_method	man
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	8580

Outer membrane protein OmpW

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

Outer membrane protein W

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

2f1v__assembly_10__model_1

2f1v__assembly_10__model_1 | I(q)

2f1v__assembly_10__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 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)

Source organism organism	Escherichia coli K12
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	Escherichia coli

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	6

Outer membrane protein OmpW

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

Outer membrane protein W

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

2f1v__assembly_10__model_1

2f1v__assembly_10__model_1 | I(q)

2f1v__assembly_10__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 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)