2atq

RB69 single-stranded DNA binding protein-DNA polymerase fusion

Method: X-RAY DIFFRACTION Dmax: 133.4 Å Quality: GOOD

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

DNA polymerase

Enterobacteria phage RB69

UniProt Q38087

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–903 Mutation:D222A, D327A gp32 × 1 (Q7Y265) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;PEG 400, Tris-Cl, 6-aminocaproic acid, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.20 Å R-free 0.345

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.

120 other PDB entries and 166 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOL_BPR69
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–903; UniProt 1–903

gp32

Enterobacteria phage RB69

UniProt Q7Y265

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 21–253 Fragment:RB69 single-stranded DNA binding protein DNA polymerase × 1 (Q38087) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;PEG 400, Tris-Cl, 6-aminocaproic acid, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 3.20 Å R-free 0.345

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q7Y265_BPR69
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–234; UniProt 21–253

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 2atq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2atq
Deposition date deposition_date2005-08-25
Structure title titleRB69 single-stranded DNA binding protein-DNA polymerase fusion
Keywords keywords;DNA polymerase, palm domain, fingers domain, thumb domain, single-stranded DNA binding protein, OB-fold, TRANSFERASE-DNA BINDING PROTEIN COMPLEX ;; TRANSFERASE/DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.27
Radius of gyration Rg (electron density) rg_electron37.99
Forward intensity I(0) i0224892000.00
Molecular weight molecular_weight122540.0 kDa
Excluded volume excluded_volume153970 ų
Envelope volume envelope_volume223690 ų
Hydration-shell volume shell_volume50251 ų
Envelope diameter envelope_diameter141.2
Shell Rg shell_rg42.33
Envelope Rg envelope_rg38.31
Shape Rg shape_rg37.98
Total Rg total_rg38.32
Total atoms total_atoms8636
Residues n_residues1055
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 dmax133.4
Rg (real space) rg_real38.36
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real2.2490e+08
I(0) uncertainty (real space) i0_real_error3.7270e+06
Rg (reciprocal space) rg_reciprocal38.31
I(0) (reciprocal space) i0_reciprocal224900000.0000
Solution quality estimate total_estimate0.8564
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis0.043
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21350000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.756; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2atqa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.3 — Ribonuclease H-like
Family Family familyc.55.3.5 — DnaQ-like 3'-5' exonuclease
Domain ID domain_idd2atqa2
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.8 — DNA/RNA polymerases
Superfamily Superfamily superfamilye.8.1 — DNA/RNA polymerases
Family Family familye.8.1.1 — DNA polymerase I
Domain ID domain_idd2atqb1
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.7 — Phage ssDNA-binding proteins

CATH v4.4 (6 domains)

Domain ID domain_id2atqA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology342 — DNA Polymerase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — DNA Polymerase, chain B, domain 1
Domain ID domain_id2atqA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H
Domain ID domain_id2atqA03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1600 — Palm domain of DNA polymerase
Homologous superfamily homologous superfamily10 — B family DNA polymerase, palm domain
Domain ID domain_id2atqA04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily690 — B family DNA polymerase, finger domain
Domain ID domain_id2atqA05
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily300
Domain ID domain_id2atqB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology198 — Replication Fork Single-Stranded DNA Binding Protein
Homologous superfamily homologous superfamily10 — Replication Fork Single-Stranded Dna Binding Protein

8. Citations (1)

9. Files and Curves (10)