1eoo

ECORV BOUND TO COGNATE DNA

Method: X-RAY DIFFRACTION Dmax: 75.6 Å Quality: GOOD

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

TYPE II RESTRICTION ENZYME ECORV

Escherichia coli

UniProt P04390

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 Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–244 Chain B; UniProt 1–244 Not recorded ;DNA (5'-D(*GP*AP*AP*GP*AP*TP*AP*TP*CP*TP*TP*C)-3') ; × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;297 K;1.5 M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 2.16 Å R-free 0.316

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.

31 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name T2E5_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 2–245; UniProt 1–244 Author chain B; PDBConstruct 2–245; UniProt 1–244

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 1eoo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1eoo
Deposition date deposition_date2000-03-23
Structure title titleECORV BOUND TO COGNATE DNA
Keywords keywordsprotein-DNA recognition, induced fit, endonuclease, hydrolase-DNA COMPLEX; hydrolase/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.79
Radius of gyration Rg (electron density) rg_electron23.21
Forward intensity I(0) i070153300.00
Molecular weight molecular_weight62028.0 kDa
Excluded volume excluded_volume75815 ų
Envelope volume envelope_volume86520 ų
Hydration-shell volume shell_volume30324 ų
Envelope diameter envelope_diameter79.3
Shell Rg shell_rg30.98
Envelope Rg envelope_rg23.36
Shape Rg shape_rg23.23
Total Rg total_rg23.91
Total atoms total_atoms4374
Residues n_residues512
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 dmax75.6
Rg (real space) rg_real23.67
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real7.0150e+07
I(0) uncertainty (real space) i0_real_error9.1400e+05
Rg (reciprocal space) rg_reciprocal23.70
I(0) (reciprocal space) i0_reciprocal70150000.0000
Solution quality estimate total_estimate0.8122
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.5
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14310000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1eooa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.52 — Restriction endonuclease-like
Superfamily Superfamily superfamilyc.52.1 — Restriction endonuclease-like
Family Family familyc.52.1.2 — Restriction endonuclease EcoRV
Domain ID domain_idd1eoob_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.52 — Restriction endonuclease-like
Superfamily Superfamily superfamilyc.52.1 — Restriction endonuclease-like
Family Family familyc.52.1.2 — Restriction endonuclease EcoRV

CATH v4.4 (2 domains)

Domain ID domain_id1eooA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology600 — ECO RV Endonuclease; Chain A
Homologous superfamily homologous superfamily10 — DNA mismatch repair MutH/Restriction endonuclease, type II
Domain ID domain_id1eooB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology600 — ECO RV Endonuclease; Chain A
Homologous superfamily homologous superfamily10 — DNA mismatch repair MutH/Restriction endonuclease, type II

8. Citations (1)

9. Files and Curves (10)