1stx

Structure of the K38A mutant of EcoRV bound to cognate DNA and Mn2+

Method: X-RAY DIFFRACTION Dmax: 79.7 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 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 × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;290 K;17% PEG 4000, 0.1M HEPES pH 7.5, 0.15M NaCl 50mM MnCl2, Vapor diffusion, temperature 290K Resolution 2.10 Å R-free 0.262

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 1stx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1stx
Deposition date deposition_date2004-03-25
Structure title titleStructure of the K38A mutant of EcoRV bound to cognate DNA and Mn2+
Keywords keywordsrestriction enzyme; EcoRV; DNA; X-ray crystallography, 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_guinier23.93
Radius of gyration Rg (electron density) rg_electron23.40
Forward intensity I(0) i070701800.00
Molecular weight molecular_weight62976.0 kDa
Excluded volume excluded_volume77288 ų
Envelope volume envelope_volume88342 ų
Hydration-shell volume shell_volume30662 ų
Envelope diameter envelope_diameter80.4
Shell Rg shell_rg31.28
Envelope Rg envelope_rg23.65
Shape Rg shape_rg23.43
Total Rg total_rg24.08
Total atoms total_atoms4423
Residues n_residues510
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 dmax79.7
Rg (real space) rg_real23.82
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real7.0700e+07
I(0) uncertainty (real space) i0_real_error9.4900e+05
Rg (reciprocal space) rg_reciprocal23.85
I(0) (reciprocal space) i0_reciprocal70700000.0000
Solution quality estimate total_estimate0.7927
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.314
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16920000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.777; Stabil: 0.990; Sysdev: 1.000; 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_idd1stxa_
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_idd1stxb_
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_id1stxA00
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_id1stxB00
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)