10xo

Streptomyces lividans DnaA DI protein in the P6(1)22 space group

Method: X-RAY DIFFRACTION Dmax: 39.3 Å Quality: EXCELLENT

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

Chromosomal replication initiator protein DnaA

Streptomyces lividans

UniProt A0A7U9DVX7

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 1–90 Not recorded CHLORIDE ION × 2 GLYCEROL × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.264

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7U9DVX7_STRLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–93; UniProt 1–90

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 10xo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id10xo
Deposition date deposition_date2026-02-11
最后修订 last_revision2026-06-03
Structure title titleStreptomyces lividans DnaA DI protein in the P6(1)22 space group
Keywords keywordsInitiator, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.22
Radius of gyration Rg (electron density) rg_electron11.70
Forward intensity I(0) i01769060.00
Molecular weight molecular_weight9048.0 kDa
Excluded volume excluded_volume11377 ų
Envelope volume envelope_volume12425 ų
Hydration-shell volume shell_volume9255 ų
Envelope diameter envelope_diameter36.6
Shell Rg shell_rg17.10
Envelope Rg envelope_rg11.86
Shape Rg shape_rg11.71
Total Rg total_rg13.04
Total atoms total_atoms635
Residues n_residues84
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax39.3
Rg (real space) rg_real13.10
Rg uncertainty (real space) rg_real_error0.16
I(0) (real space) i0_real1.7690e+06
I(0) uncertainty (real space) i0_real_error1.5930e+04
Rg (reciprocal space) rg_reciprocal13.11
I(0) (reciprocal space) i0_reciprocal1769000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.004
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha263500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)