1eop

ECORV BOUND TO COGNATE DNA

Method: X-RAY DIFFRACTION Dmax: 76.3 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 4.5;290 K;25% PEG 4000, 0.1 M acetate, 0.2 M tartrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.60 Å R-free 0.302

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 1eop

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1eop
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_guinier23.96
Radius of gyration Rg (electron density) rg_electron23.32
Forward intensity I(0) i066316300.00
Molecular weight molecular_weight60821.0 kDa
Excluded volume excluded_volume74736 ų
Envelope volume envelope_volume87695 ų
Hydration-shell volume shell_volume30555 ų
Envelope diameter envelope_diameter77.8
Shell Rg shell_rg31.12
Envelope Rg envelope_rg23.44
Shape Rg shape_rg23.33
Total Rg total_rg24.07
Total atoms total_atoms4289
Residues n_residues501
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 dmax76.3
Rg (real space) rg_real23.83
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real6.6320e+07
I(0) uncertainty (real space) i0_real_error8.0320e+05
Rg (reciprocal space) rg_reciprocal23.86
I(0) (reciprocal space) i0_reciprocal66320000.0000
Solution quality estimate total_estimate0.8910
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.8
Skewness Skewness skewness0.243
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16770000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.987

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_idd1eopa_
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_idd1eopb_
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_id1eopA00
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_id1eopB00
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)