2dwl

Crystal structure of the PriA protein complexed with oligonucleotides

Method: X-RAY DIFFRACTION Dmax: 88.0 Å Quality: REASONABLE

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

Primosomal protein N

Escherichia coli

UniProt P17888

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–DNA Homooligomer Protein × 2 DNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 1–105 Chain B; UniProt 1–105 Fragment:Residues 1-105 5'-D(*AP*(DC))-3' × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 3.8;293 K;0.1M sodium citrate, 0.2M ammonium sulfate, pH 3.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.20 Å R-free 0.302
2 Protein–DNA Homooligomer Protein × 2 DNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain C; UniProt 1–105 Chain D; UniProt 1–105 Fragment:Residues 1-105 5'-D(*AP*(DC))-3' × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 3.8;293 K;0.1M sodium citrate, 0.2M ammonium sulfate, pH 3.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.20 Å R-free 0.302

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.

9 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRIA_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–105; UniProt 1–105 Author chain B; PDBConstruct 1–105; UniProt 1–105 Author chain C; PDBConstruct 1–105; UniProt 1–105 Author chain D; PDBConstruct 1–105; UniProt 1–105

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 2dwl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2dwl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2dwl
Deposition date deposition_date2006-08-15
Structure title titleCrystal structure of the PriA protein complexed with oligonucleotides
Keywords keywordsPROTEIN-DNA COMPLEX, HYDROLASE-DNA COMPLEX; HYDROLASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.87
Radius of gyration Rg (electron density) rg_electron26.49
Forward intensity I(0) i033907300.00
Molecular weight molecular_weight47709.0 kDa
Excluded volume excluded_volume60941 ų
Envelope volume envelope_volume77902 ų
Hydration-shell volume shell_volume25510 ų
Envelope diameter envelope_diameter89.7
Shell Rg shell_rg32.60
Envelope Rg envelope_rg26.48
Shape Rg shape_rg26.50
Total Rg total_rg27.22
Total atoms total_atoms3373
Residues n_residues421
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 dmax88.0
Rg (real space) rg_real26.95
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real3.3910e+07
I(0) uncertainty (real space) i0_real_error5.1110e+05
Rg (reciprocal space) rg_reciprocal26.93
I(0) (reciprocal space) i0_reciprocal33910000.0000
Solution quality estimate total_estimate0.7007
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.399
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8832000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 0.199; Positv: 1.000; Valcen: 0.908; Smooth: 0.923

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id2dwlA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1440 — GIY-YIG endonuclease
Homologous superfamily homologous superfamily60 — PriA, 3(prime) DNA-binding domain
Domain ID domain_id2dwlB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1440 — GIY-YIG endonuclease
Homologous superfamily homologous superfamily60 — PriA, 3(prime) DNA-binding domain
Domain ID domain_id2dwlC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1440 — GIY-YIG endonuclease
Homologous superfamily homologous superfamily60 — PriA, 3(prime) DNA-binding domain
Domain ID domain_id2dwlD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1440 — GIY-YIG endonuclease
Homologous superfamily homologous superfamily60 — PriA, 3(prime) DNA-binding domain

8. Citations (1)

9. Files and Curves (10)