10xk

Bifidobacterium primatium DnaA DI

Method: X-RAY DIFFRACTION Dmax: 97.3 Å Quality: EXCELLENT

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

Chromosomal replication initiator protein DnaA

Bifidobacterium primatium

UniProt A0A2M9HC27

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 1–87 Chain E; UniProt 1–87 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å R-free 0.236
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–87 Chain D; UniProt 1–87 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å R-free 0.236
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–87 Chain F; UniProt 1–87 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å R-free 0.236
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–87 Chain H; UniProt 1–87 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å R-free 0.236

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 A0A2M9HC27_9BIFI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–90; UniProt 1–87 Author chain B; PDBConstruct 4–90; UniProt 1–87 Author chain C; PDBConstruct 4–90; UniProt 1–87 Author chain D; PDBConstruct 4–90; UniProt 1–87 Author chain E; PDBConstruct 4–90; UniProt 1–87 Author chain F; PDBConstruct 4–90; UniProt 1–87 Author chain G; PDBConstruct 4–90; UniProt 1–87 Author chain H; PDBConstruct 4–90; UniProt 1–87

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 10xk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id10xk
Deposition date deposition_date2026-02-11
最后修订 last_revision2026-06-03
Structure title titleBifidobacterium primatium DnaA DI
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_guinier31.13
Radius of gyration Rg (electron density) rg_electron30.52
Forward intensity I(0) i091875300.00
Molecular weight molecular_weight73914.0 kDa
Excluded volume excluded_volume92101 ų
Envelope volume envelope_volume126110 ų
Hydration-shell volume shell_volume35525 ų
Envelope diameter envelope_diameter105.5
Shell Rg shell_rg36.57
Envelope Rg envelope_rg29.90
Shape Rg shape_rg30.50
Total Rg total_rg31.18
Total atoms total_atoms5175
Residues n_residues689
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 dmax97.3
Rg (real space) rg_real30.96
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real9.1880e+07
I(0) uncertainty (real space) i0_real_error1.3350e+06
Rg (reciprocal space) rg_reciprocal31.04
I(0) (reciprocal space) i0_reciprocal91880000.0000
Solution quality estimate total_estimate0.9089
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.0
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9062000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)