3v7j

Co-crystal structure of Wild Type Rat polymerase beta: Enzyme-DNA binary complex

Method: X-RAY DIFFRACTION Dmax: 72.3 Å Quality: EXCELLENT

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

DNA polymerase beta

Rattus norvegicus

UniProt P06766

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 Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 4–335 Not recorded ;DNA (5'-D(P*AP*TP*GP*TP*GP*AP*GP*T)-3') ; × 1 ;DNA (5'-D(P*CP*AP*AP*AP*CP*TP*CP*AP*CP*AP*TP*A)-3') ; × 1 NA SODIUM ION × 8 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;296 K;PEG 3350, NaCl, Glycerol, Cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 296K Resolution 2.25 Å R-free 0.243

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.

30 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOLB_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–340; UniProt 4–335

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 3v7j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3v7j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3v7j
Deposition date deposition_date2011-12-21
Structure title titleCo-crystal structure of Wild Type Rat polymerase beta: Enzyme-DNA binary complex
Keywords keywordsProtein-DNA complex, repair polymerase, Transferase-DNA complex; Transferase/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.53
Radius of gyration Rg (electron density) rg_electron23.01
Forward intensity I(0) i037770100.00
Molecular weight molecular_weight43666.0 kDa
Excluded volume excluded_volume53021 ų
Envelope volume envelope_volume68910 ų
Hydration-shell volume shell_volume24999 ų
Envelope diameter envelope_diameter75.4
Shell Rg shell_rg30.11
Envelope Rg envelope_rg22.92
Shape Rg shape_rg23.00
Total Rg total_rg23.84
Total atoms total_atoms3037
Residues n_residues347
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 dmax72.3
Rg (real space) rg_real23.40
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real3.7770e+07
I(0) uncertainty (real space) i0_real_error4.9210e+05
Rg (reciprocal space) rg_reciprocal23.43
I(0) (reciprocal space) i0_reciprocal37770000.0000
Solution quality estimate total_estimate0.9110
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.5
Skewness Skewness skewness0.147
Kurtosis Kurtosis kurtosis-0.485
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4780000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3v7ja1
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.6 — DNA polymerase beta, N-terminal domain-like
Family Family familya.60.6.1 — DNA polymerase beta, N-terminal domain-like
Domain ID domain_idd3v7ja2
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.12 — PsbU/PolX domain-like
Family Family familya.60.12.1 — DNA polymerase beta-like, second domain
Domain ID domain_idd3v7ja3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.218 — Nucleotidyltransferase
Superfamily Superfamily superfamilyd.218.1 — Nucleotidyltransferase
Family Family familyd.218.1.2 — DNA polymerase beta-like

CATH v4.4 (4 domains)

Domain ID domain_id3v7jA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily110 — DNA polymerase beta, N-terminal domain-like
Domain ID domain_id3v7jA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily20 — 5' to 3' exonuclease, C-terminal subdomain
Domain ID domain_id3v7jA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology460 — Beta Polymerase; domain 2
Homologous superfamily homologous superfamily10 — Beta Polymerase, domain 2
Domain ID domain_id3v7jA04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology210 — Beta Polymerase; domain 3
Homologous superfamily homologous superfamily10 — DNA polymerase, thumb domain

8. Citations (1)

9. Files and Curves (10)