SAXSdb — 1g8e

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

FLAGELLAR TRANSCRIPTIONAL ACTIVATOR FLHD

Escherichia coli

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FLHD_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–116； UniProt 4–119 Author chain B； PDBConstruct 1–116； UniProt 4–119

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	1g8e
Deposition date deposition_date	2000-11-17
Structure title title	CRYSTAL STRUCTURE OF FLHD FROM ESCHERICHIA COLI
Keywords keywords	genetic regulator, DNA binding protein, TRANSCRIPTION; TRANSCRIPTION
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.

1g8e__assembly_1__model_1

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

Download this curve (.dat)

1g8e__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1g8e__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.96 Å
Rg (electron density)	16.72 Å
Total Rg	17.76 Å
Atom count	1418
Residues	178
Excluded volume	25485 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1g8e__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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1g8ea_
Class class	a — All alpha proteins
Fold Fold fold	a.145 — Flagellar transcriptional activator FlhD
Superfamily Superfamily superfamily	a.145.1 — Flagellar transcriptional activator FlhD
Family Family family	a.145.1.1 — Flagellar transcriptional activator FlhD

Domain ID domain_id	d1g8eb_
Class class	a — All alpha proteins
Fold Fold fold	a.145 — Flagellar transcriptional activator FlhD
Superfamily Superfamily superfamily	a.145.1 — Flagellar transcriptional activator FlhD
Family Family family	a.145.1.1 — Flagellar transcriptional activator FlhD

CATH v4.4 (2 domains)

Domain ID domain_id	1g8eA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	4000 — Flagellar transcriptional activator fold
Homologous superfamily homologous superfamily	10 — Flagellar transcriptional activator FlhD

Domain ID domain_id	1g8eB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	4000 — Flagellar transcriptional activator fold
Homologous superfamily homologous superfamily	10 — Flagellar transcriptional activator FlhD

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Unit-cell length a length_a	88.717 Å
Unit-cell length b length_b	88.717 Å
Unit-cell length c length_c	42.423 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	16

Space group space_group	I 4
Space-group number int_tables_number	79
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.2180
R_work r_work	0.2180
R_free r_free	0.2990

Description description	FLAGELLAR TRANSCRIPTIONAL ACTIVATOR FLHD
Molecular weight formula_weight	13333.4 kDa
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	1535

CRYSTAL STRUCTURE OF FLHD FROM ESCHERICHIA COLI

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

FLAGELLAR TRANSCRIPTIONAL ACTIVATOR FLHD

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

1g8e__assembly_1__model_1

1g8e__assembly_1__model_1 | I(q)

1g8e__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	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
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	117

CRYSTAL STRUCTURE OF FLHD FROM ESCHERICHIA COLI

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

FLAGELLAR TRANSCRIPTIONAL ACTIVATOR FLHD

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

1g8e__assembly_1__model_1

1g8e__assembly_1__model_1 | I(q)

1g8e__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)