SAXSdb — 1ov9

▼

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

VicH protein

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	Q9KSX6_VIBCH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–50； UniProt 2–51 Author chain B； PDBConstruct 1–50； UniProt 2–51

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1ov9
Deposition date deposition_date	2003-03-26
Structure title title	Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS protein from Vibrio cholerae
Keywords keywords	dimer, helix, coiled-coil, DNA binding protein; DNA BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1ov9__assembly_1__model_1

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

Download this curve (.dat)

1ov9__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1ov9__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	15.38 Å
Rg (electron density)	13.91 Å
Total Rg	15.02 Å
Atom count	752
Residues	93
Excluded volume	13448 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1ov9__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (2)

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1ov9a_
Class class	a — All alpha proteins
Fold Fold fold	a.155 — H-NS histone-like proteins
Superfamily Superfamily superfamily	a.155.1 — H-NS histone-like proteins
Family Family family	a.155.1.1 — H-NS histone-like proteins

Domain ID domain_id	d1ov9b_
Class class	a — All alpha proteins
Fold Fold fold	a.155 — H-NS histone-like proteins
Superfamily Superfamily superfamily	a.155.1 — H-NS histone-like proteins
Family Family family	a.155.1.1 — H-NS histone-like proteins

CATH v4.4 (2 domains)

Domain ID domain_id	1ov9A00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	1050 — H-NS histone-like proteins

Domain ID domain_id	1ov9B00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	1050 — H-NS histone-like proteins

▶

Unit-cell length a length_a	37.085 Å
Unit-cell length b length_b	49.192 Å
Unit-cell length c length_c	101.389 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	I 2 2 2
Space-group number int_tables_number	23
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2580
R_work r_work	0.2330
R_free r_free	0.2690

Description description	VicH protein
Molecular weight formula_weight	5751.5 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	799

Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS protein from Vibrio cholerae

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

VicH 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

1ov9__assembly_1__model_1

1ov9__assembly_1__model_1 | I(q)

1ov9__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 BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	47

Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS protein from Vibrio cholerae

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

VicH 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

1ov9__assembly_1__model_1

1ov9__assembly_1__model_1 | I(q)

1ov9__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)