SAXSdb — 3nvr

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

Methyl-accepting chemotaxis protein

Thermoanaerobacter tengcongensis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	PROTOPORPHYRIN IX CONTAINING FE × 2 OXYGEN MOLECULE × 2 CHLORIDE ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8RBX6_THETN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–188； UniProt 1–188 Author chain B； PDBConstruct 1–188； UniProt 1–188

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	3nvr
Deposition date deposition_date	2010-07-08
Structure title title	Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion
Keywords keywords	H-NOX, Hemoprotein, Heme cofactor, Signaling Protein; 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.

3nvr__assembly_1__model_1

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

Download this curve (.dat)

3nvr__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3nvr__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.14 Å
Rg (electron density)	22.94 Å
Total Rg	23.83 Å
Atom count	3027
Residues	358
Excluded volume	54455 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3nvr__assembly_1__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 (5)

Entity 1 Entity 1 polymer

Description description	Methyl-accepting chemotaxis protein
Molecular weight formula_weight	22047.5 kDa
Mutation mutation	I5L
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3082

MKGTLVGTWIKTLRDLYGNDVVDESLKSVGWEPDRVITPLEDIDDDEVRRIFAKVSEKTGKNVNEIWREVGRQNIKTFSEWFPSYFAGRRLVNFLMMMDEVHLQLTKMIKGATPPRLIAKPVAKDAIEMEYVSKRKMYDYFLGLIEGSSKFFKEEISVEEVERGEKDGFSRLKVRIKFKNPVFEYKKN

Source Source

Source organism organism	Thermoanaerobacter tengcongensis
NCBI taxonomy ID ncbi_taxonomy_id	119072
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	PROTOPORPHYRIN IX CONTAINING FE
Molecular weight formula_weight	616.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	OXYGEN MOLECULE
Molecular weight formula_weight	32.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	55

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3nvra_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.278 — Ligand-binding domain in the NO signalling and Golgi transport
Superfamily Superfamily superfamily	d.278.1 — Ligand-binding domain in the NO signalling and Golgi transport
Family Family family	d.278.1.1 — H-NOX domain

Domain ID domain_id	d3nvrb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.278 — Ligand-binding domain in the NO signalling and Golgi transport
Superfamily Superfamily superfamily	d.278.1 — Ligand-binding domain in the NO signalling and Golgi transport
Family Family family	d.278.1.1 — H-NOX domain

CATH v4.4 (2 domains)

Domain ID domain_id	3nvrA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1520 — H-NOX domain
Homologous superfamily homologous superfamily	10 — H-NOX domain

Domain ID domain_id	3nvrB00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1520 — H-NOX domain
Homologous superfamily homologous superfamily	10 — H-NOX domain

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Unit-cell length a length_a	79.825 Å
Unit-cell length b length_b	126.095 Å
Unit-cell length c length_c	42.742 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	8

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.148 Å
Low-resolution limit resolution_low	49.477 Å
R factor r_factor	0.2194
R_work r_work	0.2172
R_free r_free	0.2599

Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion

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

Methyl-accepting chemotaxis protein

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

3nvr__assembly_1__model_1

3nvr__assembly_1__model_1 | I(q)

3nvr__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion

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

Methyl-accepting chemotaxis protein

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

3nvr__assembly_1__model_1

3nvr__assembly_1__model_1 | I(q)

3nvr__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)