SAXSdb — 1uv7

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

GENERAL SECRETION PATHWAY PROTEIN M

VIBRIO CHOLERAE

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	GSPM_VIBCH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–102； UniProt 65–165 Author chain B； PDBConstruct 2–102； UniProt 65–165

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	1uv7
Deposition date deposition_date	2004-01-15
Structure title title	periplasmic domain of EpsM from Vibrio cholerae
Keywords keywords	GENERAL SECRETION PATHWAY, VIBRIO CHOLERAE, TRANSPORT; TRANSPORT
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.

1uv7__assembly_1__model_1

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

Download this curve (.dat)

1uv7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1uv7__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.51 Å
Rg (electron density)	16.09 Å
Total Rg	17.18 Å
Atom count	1228
Residues	146
Excluded volume	22078 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1uv7__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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1uv7a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.67 — RRF/tRNA synthetase additional domain-like
Superfamily Superfamily superfamily	d.67.4 — General secretion pathway protein M, EpsM
Family Family family	d.67.4.1 — General secretion pathway protein M, EpsM

Domain ID domain_id	d1uv7b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.67 — RRF/tRNA synthetase additional domain-like
Superfamily Superfamily superfamily	d.67.4 — General secretion pathway protein M, EpsM
Family Family family	d.67.4.1 — General secretion pathway protein M, EpsM

CATH v4.4 (2 domains)

Domain ID domain_id	1uv7A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	100 — General secretion pathway protein M, EpsM

Domain ID domain_id	1uv7B00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	100 — General secretion pathway protein M, EpsM

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Unit-cell length a length_a	52.879 Å
Unit-cell length b length_b	52.879 Å
Unit-cell length c length_c	112.484 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 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.1960
R_free r_free	0.2420

Description description	GENERAL SECRETION PATHWAY PROTEIN M
Molecular weight formula_weight	12639.8 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	1314

periplasmic domain of EpsM from Vibrio cholerae

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

GENERAL SECRETION PATHWAY PROTEIN M

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

1uv7__assembly_1__model_1

1uv7__assembly_1__model_1 | I(q)

1uv7__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Source organism organism	VIBRIO CHOLERAE
NCBI taxonomy ID ncbi_taxonomy_id	666
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	70

periplasmic domain of EpsM from Vibrio cholerae

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

GENERAL SECRETION PATHWAY PROTEIN M

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

1uv7__assembly_1__model_1

1uv7__assembly_1__model_1 | I(q)

1uv7__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)