SAXSdb — 9z71

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

Winged helix-turn-helix transcriptional regulator

Enterobacter roggenkampii

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 2–182	Not recorded	SULFATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.55 Å R-free 0.190

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A443UND6_ENTCL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–184； UniProt 2–182

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	9z71
Deposition date deposition_date	2025-11-15
Structure title title	Structure of E. roggenkampii CapS
Keywords keywords	transcription factor, STAS domain, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	17.75 Å
Radius of gyration Rg (electron density) rg_electron	16.55 Å
Forward intensity I(0) i0	7221480.00
Molecular weight molecular_weight	19586.0 kDa
Excluded volume excluded_volume	24563 Å³
Envelope volume envelope_volume	27873 Å³
Hydration-shell volume shell_volume	14658 Å³
Envelope diameter envelope_diameter	59.2 Å
Shell Rg shell_rg	22.00 Å
Envelope Rg envelope_rg	16.82 Å
Shape Rg shape_rg	16.55 Å
Total Rg total_rg	17.51 Å
Total atoms total_atoms	2776
Residues n_residues	181
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	58.1 Å
Rg (real space) rg_real	17.73 Å
Rg uncertainty (real space) rg_real_error	0.42 Å
I(0) (real space) i0_real	7.2210e+06
I(0) uncertainty (real space) i0_real_error	8.0850e+04
Rg (reciprocal space) rg_reciprocal	17.73 Å
I(0) (reciprocal space) i0_reciprocal	7221000.0000
Solution quality estimate total_estimate	0.8017
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.9 Å
Skewness Skewness skewness	0.351
Kurtosis Kurtosis kurtosis	-0.203
Angular range angular_range	— – 0.4500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1305000.0000
Real-space data points n_real_points	76
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Winged helix-turn-helix transcriptional regulator
Molecular weight formula_weight	19684.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3017

SNAKVKLLELTENNNHPFGNVLGREVFKRLQNVVDSNPGCKSFEISLEGIVATDSSFPRESVIALAKQLCGEKYFFITDVSSTDLIDNWDYAAIAKQQSMIVVLAGGVRVIGPEAKSSTKALLDVVLGRNGVSTANVAKSLNISVQNASTRLKKLSSEGVIMRSEVSSPTGGIEFIYSGPNISA

来源 Source

来源生物 organism	Enterobacter roggenkampii
NCBI Class编号 ncbi_taxonomy_id	1812935
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	203

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8. Citations (1)

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Unit-cell length a length_a	55.826 Å
Unit-cell length b length_b	55.826 Å
Unit-cell length c length_c	184.515 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 65 2 2
Space-group number int_tables_number	179
Crystal system crystal_system	hexagonal

Resolution resolution	1.550 Å
Low-resolution limit resolution_low	29.330 Å
R factor r_factor	0.1678
R_work r_work	0.1666
R_free r_free	0.1902

fit	/app/data/saxs_computation/z7/9z71/9z71.fit
pddf	/app/data/pr_computation/z7/9z71/9z71.pr.out
profile	/app/data/saxs_computation/z7/9z71/9z71.dat

Structure of E. roggenkampii CapS

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

Winged helix-turn-helix transcriptional regulator

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction