1clq

CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 105.5 Å Quality: GOOD

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

PROTEIN (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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 1–903 Fragment:RESIDUES 1-903 ;DNA (5'-D(*GP*CP*GP*GP*AP*AP*CP*TP*AP*CP*T)-3') ; × 1 ;DNA (5'-D(*AP*GP*TP*AP*GP*TP*TP*CP*CP*GP*CP*G)-3') ; × 1 CA CALCIUM ION × 9 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;285 K;12% (W/V) PEG 350MME, 150 MM CACL2, 100 MM SODIUM CACODYLATE, PH 6.5, 12 DEGREES C, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 2.70 Å R-free 0.284

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 3
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 1clq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1clq
Deposition date deposition_date1999-04-30
Structure title titleCRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION
Keywords keywordsDNA POLYMERASE, GP43, PROOFREADING, EDITING, REPLICATION, 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_guinier33.02
Radius of gyration Rg (electron density) rg_electron32.15
Forward intensity I(0) i0208109000.00
Molecular weight molecular_weight112430.0 kDa
Excluded volume excluded_volume139380 ų
Envelope volume envelope_volume185830 ų
Hydration-shell volume shell_volume47211 ų
Envelope diameter envelope_diameter113.1
Shell Rg shell_rg40.02
Envelope Rg envelope_rg31.71
Shape Rg shape_rg32.15
Total Rg total_rg32.78
Total atoms total_atoms7885
Residues n_residues926
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 dmax105.5
Rg (real space) rg_real32.76
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real2.0810e+08
I(0) uncertainty (real space) i0_real_error3.3720e+06
Rg (reciprocal space) rg_reciprocal32.88
I(0) (reciprocal space) i0_reciprocal208100000.0000
Solution quality estimate total_estimate0.8965
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.0
Skewness Skewness skewness0.063
Kurtosis Kurtosis kurtosis-0.532
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22570000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1clqa1
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_idd1clqa2
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_id1clqA01
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_id1clqA02
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_id1clqA03
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_id1clqA04
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_id1clqA05
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily300
Domain ID domain_id1clqA06
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 (1)

9. Files and Curves (10)