1sx5

K38A EcoRV bound to cleaved DNA and Mn2+: P1 crystal form

Method: X-RAY DIFFRACTION Dmax: 77.9 Å Quality: REASONABLE

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 4 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–244 Chain B; UniProt 1–244 Mutation:K38A 5'-D(*AP*AP*AP*GP*AP*T)-3' × 2 5'-D(P*AP*TP*CP*TP*T)-3' × 2 MN MANGANESE (II) ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;315 K;PEG 4000, 0.1M HEPES, 0.15M NaCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 315K Resolution 1.50 Å R-free 0.254

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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–244; UniProt 1–244 Author chain B; PDBConstruct 1–244; 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 1sx5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1sx5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1sx5
Deposition date deposition_date2004-03-30
Structure title titleK38A EcoRV bound to cleaved DNA and Mn2+: P1 crystal form
Keywords keywordsendonuclease, protein-DNA complex, 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_electron23.25
Forward intensity I(0) i068608700.00
Molecular weight molecular_weight61609.0 kDa
Excluded volume excluded_volume75378 ų
Envelope volume envelope_volume86934 ų
Hydration-shell volume shell_volume30341 ų
Envelope diameter envelope_diameter80.2
Shell Rg shell_rg31.05
Envelope Rg envelope_rg23.50
Shape Rg shape_rg23.29
Total Rg total_rg23.91
Total atoms total_atoms4321
Residues n_residues504
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 dmax77.9
Rg (real space) rg_real23.67
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real6.8610e+07
I(0) uncertainty (real space) i0_real_error9.1310e+05
Rg (reciprocal space) rg_reciprocal23.70
I(0) (reciprocal space) i0_reciprocal68610000.0000
Solution quality estimate total_estimate0.6403
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.327
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16890000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 0.999; Sysdev: 0.286; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1sx5a_
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_idd1sx5b_
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_id1sx5A00
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_id1sx5B00
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)