2y21

The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291V mutant

Method: X-RAY DIFFRACTION

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

HAMP

ARCHAEOGLOBUS FULGIDUS

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
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
6	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	O28769_ARCFU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–56； UniProt 278–331 Author chain B； PDBConstruct 3–56； UniProt 278–331 Author chain C； PDBConstruct 3–56； UniProt 278–331 Author chain D； PDBConstruct 3–56； UniProt 278–331 Author chain E； PDBConstruct 3–56； UniProt 278–331 Author chain F； PDBConstruct 3–56； UniProt 278–331 Author chain G； PDBConstruct 3–56； UniProt 278–331 Author chain H； PDBConstruct 3–56； UniProt 278–331 Author chain I； PDBConstruct 3–56； UniProt 278–331 Author chain J； PDBConstruct 3–56； UniProt 278–331 Author chain K； PDBConstruct 3–56； UniProt 278–331 Author chain L； PDBConstruct 3–56； 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2y21
Deposition date deposition_date	2010-12-12
Structure title title	The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291V mutant
Keywords keywords	MEMBRANE PROTEIN, TRANSMEMBRANE SIGNALLING; MEMBRANE 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.

2y21__assembly_4__model_1

Assembly 4 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2y21__assembly_4__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2y21__assembly_4__model_1 | P(r) · Pending

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

Rg（Guinier）	14.80 Å
Rg (electron density)	13.27 Å
Total Rg	14.65 Å
Atom count	844
Residues	109
Excluded volume	15011 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2y21__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2y21__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2y21__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2y21__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`2y21__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`2y21__assembly_6__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) 29 domains

SCOP 2.08 (17 domains)

Domain ID domain_id	d2y21a_
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	d2y21b1
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	d2y21b2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2y21c_
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	d2y21d1
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	d2y21d2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2y21e_
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	d2y21f1
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	d2y21f2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2y21g_
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	d2y21h_
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	d2y21i_
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	d2y21j1
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	d2y21j2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2y21k_
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	d2y21l1
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	d2y21l2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (12 domains)

Domain ID domain_id	2y21A00
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	2y21B00
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	2y21C00
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	2y21D00
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	2y21E00
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	2y21F00
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	2y21G00
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	2y21H00
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	2y21I00
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	2y21J00
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	2y21K00
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	2y21L00
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

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Unit-cell length a length_a	41.150 Å
Unit-cell length b length_b	81.780 Å
Unit-cell length c length_c	206.730 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	48

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.450 Å
Low-resolution limit resolution_low	19.950 Å
R factor r_factor	0.2482
R_work r_work	0.2461
R_free r_free	0.2887

Description description	HAMP
Molecular weight formula_weight	6305.2 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	12

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L
Atom count atom_count	4966

The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291V mutant

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

HAMP

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

2y21__assembly_4__model_1

2y21__assembly_4__model_1 | I(q)

2y21__assembly_4__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) 29 domains

SCOP 2.08 (17 domains)

CATH v4.4 (12 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	61

The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291V mutant

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

HAMP

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

2y21__assembly_4__model_1

2y21__assembly_4__model_1 | I(q)

2y21__assembly_4__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) 29 domains

SCOP 2.08 (17 domains)

CATH v4.4 (12 domains)

7. Citations (1)