SAXSdb — 3zrw

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

AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ

ESCHERICHIA COLI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2	water × 2	Consistent with protein count
2	Insufficient information	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, 2
Chains and sequence ranges	Author chain A； PDBConstruct 5–54； UniProt 278–327 Author chain C； PDBConstruct 5–54； UniProt 278–327 Author chain D； PDBConstruct 5–54； UniProt 278–327 Author chain B； PDBConstruct 5–54； UniProt 278–327

AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ

ESCHERICHIA COLI

UniProt P0AEJ4

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2	water × 2	Consistent with protein count
2	Insufficient information	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	ENVZ_ECOLI
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 55–115； UniProt 229–289 Author chain C； PDBConstruct 55–115； UniProt 229–289 Author chain D； PDBConstruct 55–115； UniProt 229–289 Author chain B； PDBConstruct 55–115； UniProt 229–289

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	3zrw
Deposition date deposition_date	2011-06-20
Structure title title	The structure of the dimeric Hamp-Dhp fusion A291V mutant
Keywords keywords	SIGNALING PROTEIN, OSMOREGULATION, OMPR, OMPC; SIGNALING 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.

3zrw__assembly_1__model_1

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

Download this curve (.dat)

3zrw__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3zrw__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.80 Å
Rg (electron density)	25.80 Å
Total Rg	26.24 Å
Atom count	1730
Residues	221
Excluded volume	30643 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3zrw__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3zrw__assembly_2__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 (3)

Entity 1 Entity 1 polymer

Description description	AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ
Molecular weight formula_weight	13136.9 kDa
EC 编号 ec_number	2.7.13.3
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,D
Atom count atom_count	3714

GSHMSTITRPIIELSNTVDKIAEGNLEAEVPHQNRADEIGILAKSIERLRRSLKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRT

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ
Molecular weight formula_weight	13151.9 kDa
EC 编号 ec_number	2.7.13.3
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GSHMSTITRPIIELSNTVDKIAEGNLEAEVPHQNRADEIGILAKSIERLRRSLKQQADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRT

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	226

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	3zrwA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	130 — Signal transduction histidine kinase, dimerisation/phosphotransfer (DHp) domain

Domain ID domain_id	3zrwB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	130 — Signal transduction histidine kinase, dimerisation/phosphotransfer (DHp) domain

Domain ID domain_id	3zrwC00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	130 — Signal transduction histidine kinase, dimerisation/phosphotransfer (DHp) domain

Domain ID domain_id	3zrwD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	130 — Signal transduction histidine kinase, dimerisation/phosphotransfer (DHp) domain

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Unit-cell length a length_a	70.860 Å
Unit-cell length b length_b	46.670 Å
Unit-cell length c length_c	157.460 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	94.31 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

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

Resolution resolution	2.250 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.2170
R_work r_work	0.2141
R_free r_free	0.2695

The structure of the dimeric Hamp-Dhp fusion A291V mutant

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

AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ

State in the Current Structure

Other States of the Same Protein in the Database

AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ

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

3zrw__assembly_1__model_1

3zrw__assembly_1__model_1 | I(q)

3zrw__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

The structure of the dimeric Hamp-Dhp fusion A291V mutant

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

AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ

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

3zrw__assembly_1__model_1

3zrw__assembly_1__model_1 | I(q)

3zrw__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)