1waj

DNA POLYMERASE FROM BACTERIOPHAGE RB69

Method: X-RAY DIFFRACTION Dmax: 103.6 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–903 Not recorded 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;pH 5.6 Resolution 2.80 Å R-free 0.280

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

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 1waj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1waj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1waj
Deposition date deposition_date1997-04-13
Structure title titleDNA POLYMERASE FROM BACTERIOPHAGE RB69
Keywords keywordsNUCLEOTIDYLTRANSFERASE, RB69 DNA POLYMERASE (GP43); NUCLEOTIDYLTRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.15
Radius of gyration Rg (electron density) rg_electron31.98
Forward intensity I(0) i0167184000.00
Molecular weight molecular_weight104950.0 kDa
Excluded volume excluded_volume132050 ų
Envelope volume envelope_volume175180 ų
Hydration-shell volume shell_volume44731 ų
Envelope diameter envelope_diameter109.8
Shell Rg shell_rg39.92
Envelope Rg envelope_rg31.56
Shape Rg shape_rg31.96
Total Rg total_rg32.70
Total atoms total_atoms7404
Residues n_residues903
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 dmax103.6
Rg (real space) rg_real32.88
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real1.6720e+08
I(0) uncertainty (real space) i0_real_error2.4810e+06
Rg (reciprocal space) rg_reciprocal32.99
I(0) (reciprocal space) i0_reciprocal167200000.0000
Solution quality estimate total_estimate0.9019
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.3
Skewness Skewness skewness0.019
Kurtosis Kurtosis kurtosis-0.606
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23300000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1waja1
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_idd1waja2
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

CATH v4.4 (6 domains)

Domain ID domain_id1wajA01
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_id1wajA02
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_id1wajA03
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_id1wajA04
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_id1wajA05
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily300
Domain ID domain_id1wajA06
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1820 — Ribonuclease H-like motif
Homologous superfamily homologous superfamily10 — DnaQ-like 3'-5' exonuclease

8. Citations (5)

9. Files and Curves (10)