1cr1

CRYSTAL STRUCTURE OF THE HELICASE DOMAIN OF THE GENE 4 PROTEIN OF BACTERIOPHAGE T7: COMPLEX WITH DTTP

Method: X-RAY DIFFRACTION Dmax: 51.3 Å Quality: REASONABLE

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

DNA PRIMASE/HELICASE

Enterobacteria phage T7

UniProt P03692

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 271–566 Fragment:HELICASE DOMAIN SO4 SULFATE ION × 12 TTP THYMIDINE-5'-TRIPHOSPHATE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;298 K;AMMONIUM SULFATE, ACES, pH 9, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.30 Å R-free 0.288

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.

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRIM_BPT7
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–296; UniProt 271–566

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 1cr1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cr1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cr1
Deposition date deposition_date1999-08-12
Structure title titleCRYSTAL STRUCTURE OF THE HELICASE DOMAIN OF THE GENE 4 PROTEIN OF BACTERIOPHAGE T7: COMPLEX WITH DTTP
Keywords keywordsRECA-TYPE FOLD, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.73
Radius of gyration Rg (electron density) rg_electron18.61
Forward intensity I(0) i014373000.00
Molecular weight molecular_weight27572.0 kDa
Excluded volume excluded_volume34183 ų
Envelope volume envelope_volume40483 ų
Hydration-shell volume shell_volume18598 ų
Envelope diameter envelope_diameter76.6
Shell Rg shell_rg24.71
Envelope Rg envelope_rg19.25
Shape Rg shape_rg18.61
Total Rg total_rg19.48
Total atoms total_atoms1924
Residues n_residues245
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 dmax51.3
Rg (real space) rg_real18.77
Rg uncertainty (real space) rg_real_error0.05
I(0) (real space) i0_real1.3650e+07
I(0) uncertainty (real space) i0_real_error1.1020e+05
Rg (reciprocal space) rg_reciprocal19.73
I(0) (reciprocal space) i0_reciprocal14370000.0000
Solution quality estimate total_estimate0.6828
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.170
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha3.9260
Highest regularization parameter α highest_alpha1625000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.992; Stabil: 0.972; Sysdev: 0.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cr1a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.11 — RecA protein-like (ATPase-domain)

CATH v4.4 (1 domains)

Domain ID domain_id1cr1A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)