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10uj

Hna Monomer

Method: ELECTRON MICROSCOPY Dmax: 91.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Helicase ATP-binding domain-containing protein

Sinorhizobium meliloti

UniProt Q92XN4

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–845 Not recorded No other associated polymer ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.90 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 10UJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9YHN Hna Monomer Deposited 2025-09-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–845（845 aa）
Not recorded CA CALCIUM ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.38 Å
9YKJ Hna Dimer Deposited 2025-10-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–845（845 aa）
Chain B 1–845（845 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q92XN4_RHIME
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–845； UniProt 1–845

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.

SAXS scattering curve SAXS Profile

SAXS profile for 10uj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10uj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10uj
Deposition date deposition_date2026-02-09
Structure title titleHna Monomer
Keywords keywordsPD(D/E)XK nuclease. Superfamily 2 helicase. Anti-bacteriophage protein, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier29.35 Å
Radius of gyration Rg (electron density) rg_electron28.40 Å
Forward intensity I(0) i0135378000.00
Molecular weight molecular_weight92151.0 kDa
Excluded volume excluded_volume115620 ų
Envelope volume envelope_volume145230 ų
Hydration-shell volume shell_volume41443 ų
Envelope diameter envelope_diameter94.5 Å
Shell Rg shell_rg36.71 Å
Envelope Rg envelope_rg28.25 Å
Shape Rg shape_rg28.39 Å
Total Rg total_rg29.21 Å
Total atoms total_atoms6490
Residues n_residues821
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax91.7 Å
Rg (real space) rg_real29.23 Å
Rg uncertainty (real space) rg_real_error0.51 Å
I(0) (real space) i0_real1.3540e+08
I(0) uncertainty (real space) i0_real_error1.8940e+06
Rg (reciprocal space) rg_reciprocal29.28 Å
I(0) (reciprocal space) i0_reciprocal135400000.0000
Solution quality estimate total_estimate0.7158
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary— Å
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.404
Angular range angular_range— – 0.2700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52660000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 0.218; Positv: 1.000; Valcen: 0.988; Smooth: 0.907
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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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9. Files and Curves (10)