SAXSdb — 1qx8

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

Regulatory protein ROP

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ROP_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–58； UniProt 1–63 Author chain B； PDBConstruct 1–58； UniProt 1–63

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	1qx8
Deposition date deposition_date	2003-09-04
Structure title title	Crystal structure of a five-residue deletion mutant of the Rop protein
Keywords keywords	REPLICATION; INITIATION OF TRANSCRIPTION; RNA PRIMER; X-RAY, TRANSCRIPTION; TRANSCRIPTION
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.

1qx8__assembly_1__model_1

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

Download this curve (.dat)

1qx8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1qx8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.64 Å
Rg (electron density)	22.30 Å
Total Rg	22.94 Å
Atom count	1578
Residues	196
Excluded volume	27972 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1qx8__assembly_1__model_1`	tetrameric （4）	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	d1qx8a_
Class class	a — All alpha proteins
Fold Fold fold	a.30 — ROP-like
Superfamily Superfamily superfamily	a.30.1 — ROP protein
Family Family family	a.30.1.1 — ROP protein

Domain ID domain_id	d1qx8b_
Class class	a — All alpha proteins
Fold Fold fold	a.30 — ROP-like
Superfamily Superfamily superfamily	a.30.1 — ROP protein
Family Family family	a.30.1.1 — ROP protein

CATH v4.4 (2 domains)

Domain ID domain_id	1qx8A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	1220 — Regulatory protein rop

Domain ID domain_id	1qx8B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	1220 — Regulatory protein rop

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Unit-cell length a length_a	54.476 Å
Unit-cell length b length_b	42.565 Å
Unit-cell length c length_c	51.722 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.68 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.020 Å
Low-resolution limit resolution_low	33.000 Å
R factor r_factor	0.1906
R_work r_work	0.1895
R_free r_free	0.2122

Description description	Regulatory protein ROP
Molecular weight formula_weight	6678.5 kDa
Mutation mutation	Deletion [30D-34Q]
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	869

Crystal structure of a five-residue deletion mutant of the Rop protein

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

Regulatory protein ROP

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

1qx8__assembly_1__model_1

1qx8__assembly_1__model_1 | I(q)

1qx8__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 (2)

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
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	54

Crystal structure of a five-residue deletion mutant of the Rop protein

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

Regulatory protein ROP

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

1qx8__assembly_1__model_1

1qx8__assembly_1__model_1 | I(q)

1qx8__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 (2)