SAXSdb — 4cq4

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

ENGINEERED VERSION OF TRANSMEMBRANE RECEPTOR AF1503

ARCHAEOGLOBUS FULGIDUS

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	O28769_ARCFU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–309； UniProt 30–338 Author chain B； PDBConstruct 1–309； UniProt 30–338 Author chain C； PDBConstruct 1–309； UniProt 30–338 Author chain D； PDBConstruct 1–309； UniProt 30–338

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	4cq4
Deposition date deposition_date	2014-02-11
Structure title title	C-terminal fragment of Af1503-sol: transmembrane receptor Af1503 from Archaeoglobus fulgidus engineered for solubility
Keywords keywords	STRUCTURAL PROTEIN, HAMP DOMAIN, TWO COMPONENT SIGNAL TRANSDUCTION, TRANSMEMBRANE SIGNALLING; STRUCTURAL 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.

4cq4__assembly_1__model_1

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

Download this curve (.dat)

4cq4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4cq4__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	40.84 Å
Rg (electron density)	42.15 Å
Total Rg	41.72 Å
Atom count	3060
Residues	412
Excluded volume	54478 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4cq4__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

CATH v4.4 (4 domains)

Domain ID domain_id	4cq4A00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	340 — hypothetical protein mp506/mpn330, domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	4cq4B00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	340 — hypothetical protein mp506/mpn330, domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	4cq4C00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	340 — hypothetical protein mp506/mpn330, domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	4cq4D00
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	340 — hypothetical protein mp506/mpn330, domain 1
Homologous superfamily homologous superfamily	10 —

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Unit-cell length a length_a	44.069 Å
Unit-cell length b length_b	48.037 Å
Unit-cell length c length_c	95.187 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	98.04 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	37.670 Å
R factor r_factor	0.1954
R_work r_work	0.1929
R_free r_free	0.2430

Description description	ENGINEERED VERSION OF TRANSMEMBRANE RECEPTOR AF1503
Molecular weight formula_weight	34496.1 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	3465

C-terminal fragment of Af1503-sol: transmembrane receptor Af1503 from Archaeoglobus fulgidus engineered for solubility

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

ENGINEERED VERSION OF TRANSMEMBRANE RECEPTOR AF1503

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

4cq4__assembly_1__model_1

4cq4__assembly_1__model_1 | I(q)

4cq4__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

CATH v4.4 (4 domains)

7. Citations (1)

Source organism organism	ARCHAEOGLOBUS FULGIDUS
NCBI taxonomy ID ncbi_taxonomy_id	2234
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	382

C-terminal fragment of Af1503-sol: transmembrane receptor Af1503 from Archaeoglobus fulgidus engineered for solubility

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

ENGINEERED VERSION OF TRANSMEMBRANE RECEPTOR AF1503

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

4cq4__assembly_1__model_1

4cq4__assembly_1__model_1 | I(q)

4cq4__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

CATH v4.4 (4 domains)

7. Citations (1)