SAXSdb — 2y0t

▼

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

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 1–54； UniProt 278–331 Author chain B； PDBConstruct 1–54； UniProt 278–331

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	2y0t
Deposition date deposition_date	2010-12-07
Structure title title	The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291F mutant
Keywords keywords	MEMBRANE PROTEIN, TRANSMEMBRANE SIGNALLING; MEMBRANE 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.

2y0t__assembly_1__model_1

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

Download this curve (.dat)

2y0t__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2y0t__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	20.49 Å
Rg (electron density)	19.96 Å
Total Rg	20.69 Å
Atom count	1592
Residues	202
Excluded volume	28486 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2y0t__assembly_1__model_1`	tetrameric （4）	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	d2y0ta_
Class class	a — All alpha proteins
Fold Fold fold	a.274 — HAMP domain-like
Superfamily Superfamily superfamily	a.274.1 — HAMP domain-like
Family Family family	a.274.1.1 — HAMP domain

Domain ID domain_id	d2y0tb_
Class class	a — All alpha proteins
Fold Fold fold	a.274 — HAMP domain-like
Superfamily Superfamily superfamily	a.274.1 — HAMP domain-like
Family Family family	a.274.1.1 — HAMP domain

CATH v4.4 (2 domains)

Domain ID domain_id	2y0tA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	500 — HAMP domain in histidine kinase

Domain ID domain_id	2y0tB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	500 — HAMP domain in histidine kinase

▶

Unit-cell length a length_a	88.070 Å
Unit-cell length b length_b	34.320 Å
Unit-cell length c length_c	47.650 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	117.79 °
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	1.300 Å
Low-resolution limit resolution_low	19.560 Å
R factor r_factor	0.1749
R_work r_work	0.1731
R_free r_free	0.2086

Description description	AF1503
Molecular weight formula_weight	6083.9 kDa
Mutation mutation	YES
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	957

The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291F mutant

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

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

2y0t__assembly_1__model_1

2y0t__assembly_1__model_1 | I(q)

2y0t__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	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	119

The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291F mutant

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

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

2y0t__assembly_1__model_1

2y0t__assembly_1__model_1 | I(q)

2y0t__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)