SAXSdb — 10na

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

PilT/PilU family type 4a pilus ATPase

Vibrio cholerae

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 2–368 Chain B； UniProt 2–368 Chain C； UniProt 2–368 Chain D； UniProt 2–368 Chain E； UniProt 2–368 Chain F； UniProt 2–368	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 8.3 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.49 Å

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.

Other PDB	Difference from Current Entry 10NA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
10MY Single particle reconstruction of PilU from Vibrio cholerae El Tor E7946, form 1 Deposited 2026-01-28	Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 2–368（367 aa） Chain B 2–368（367 aa） Chain C 2–368（367 aa） Chain D 2–368（367 aa） Chain E 2–368（367 aa） Chain F 2–368（367 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.44 Å
10MZ Single particle reconstruction of PilU from Vibrio cholerae El Tor E7946, form 2 Deposited 2026-01-28	Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 2–368（367 aa） Chain B 2–368（367 aa） Chain C 2–368（367 aa） Chain D 2–368（367 aa） Chain E 2–368（367 aa） Chain F 2–368（367 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.68 Å
10NB Single particle reconstruction of PilU from Vibrio cholerae El Tor E7946, form 4 Deposited 2026-01-28	Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 2–368（367 aa） Chain B 2–368（367 aa） Chain C 2–368（367 aa） Chain D 2–368（367 aa） Chain E 2–368（367 aa） Chain F 2–368（367 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.76 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A085SZ25_VIBCL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 20–386； UniProt 2–368 Author chain B； PDBConstruct 20–386； UniProt 2–368 Author chain C； PDBConstruct 20–386； UniProt 2–368 Author chain D； PDBConstruct 20–386； UniProt 2–368 Author chain E； PDBConstruct 20–386； UniProt 2–368 Author chain F； PDBConstruct 20–386； UniProt 2–368

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	10na
Deposition date deposition_date	2026-01-28
Structure title title	Single particle reconstruction of PilU from Vibrio cholerae El Tor E7946, form 3
Keywords keywords	Retraction ATPase, Structural Genomics, Center for Structural Biology of Infectious Diseases, CSBID, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	44.14 Å
Radius of gyration Rg (electron density) rg_electron	43.42 Å
Forward intensity I(0) i0	848666000.00
Molecular weight molecular_weight	235820.0 kDa
Excluded volume excluded_volume	293940 Å³
Envelope volume envelope_volume	430630 Å³
Hydration-shell volume shell_volume	79171 Å³
Envelope diameter envelope_diameter	145.2 Å
Shell Rg shell_rg	52.26 Å
Envelope Rg envelope_rg	41.85 Å
Shape Rg shape_rg	43.42 Å
Total Rg total_rg	43.82 Å
Total atoms total_atoms	16548
Residues n_residues	2106
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	137.5 Å
Rg (real space) rg_real	43.88 Å
Rg uncertainty (real space) rg_real_error	0.83 Å
I(0) (real space) i0_real	8.4870e+08
I(0) uncertainty (real space) i0_real_error	1.4470e+07
Rg (reciprocal space) rg_reciprocal	44.14 Å
I(0) (reciprocal space) i0_reciprocal	848900000.0000
Solution quality estimate total_estimate	0.8999
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	61.1 Å
Skewness Skewness skewness	0.053
Kurtosis Kurtosis kurtosis	-0.605
Angular range angular_range	— – 0.1800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	176700000.0000
Real-space data points n_real_points	37
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.934

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.49 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	144012

Description description	PilT/PilU family type 4a pilus ATPase
Molecular weight formula_weight	42949.9 kDa
Source method src_method	man
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	16548

Single particle reconstruction of PilU from Vibrio cholerae El Tor E7946, form 3

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

PilT/PilU family type 4a pilus ATPase

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Vibrio cholerae
NCBI Class编号 ncbi_taxonomy_id	666
宿主生物 host_organism	Escherichia coli

fit	/app/data/saxs_computation/0n/10na/10na.fit
pddf	/app/data/pr_computation/0n/10na/10na.pr.out
profile	/app/data/saxs_computation/0n/10na/10na.dat