1cfr

CRYSTAL STRUCTURE OF CITROBACTER FREUNDII RESTRICTION ENDONUCLEASE CFR10I AT 2.15 ANGSTROMS RESOLUTION.

Method: X-RAY DIFFRACTION Dmax: 68.7 Å Quality: GOOD

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

RESTRICTION ENDONUCLEASE

Citrobacter freundii

UniProt P56200

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–285 Fragment:RESIDUES 1 - 283 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.5 Resolution 2.15 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name T2CX_CITFR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–285; UniProt 1–285

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 1cfr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cfr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1cfr
Deposition date deposition_date1996-02-02
Structure title titleCRYSTAL STRUCTURE OF CITROBACTER FREUNDII RESTRICTION ENDONUCLEASE CFR10I AT 2.15 ANGSTROMS RESOLUTION.
Keywords keywordsRESTRICTION ENDONUCLEASE, RESTRICTION ENZYME; RESTRICTION ENDONUCLEASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.13
Radius of gyration Rg (electron density) rg_electron20.03
Forward intensity I(0) i017071000.00
Molecular weight molecular_weight31820.0 kDa
Excluded volume excluded_volume40124 ų
Envelope volume envelope_volume47287 ų
Hydration-shell volume shell_volume20055 ų
Envelope diameter envelope_diameter71.5
Shell Rg shell_rg26.20
Envelope Rg envelope_rg20.33
Shape Rg shape_rg20.01
Total Rg total_rg20.97
Total atoms total_atoms2749
Residues n_residues283
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 dmax68.7
Rg (real space) rg_real21.07
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.7070e+07
I(0) uncertainty (real space) i0_real_error2.2590e+05
Rg (reciprocal space) rg_reciprocal21.08
I(0) (reciprocal space) i0_reciprocal17070000.0000
Solution quality estimate total_estimate0.8159
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis-0.344
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3454000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cfra_
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.52.1.7 — Cfr10I/Bse634I

CATH v4.4 (1 domains)

Domain ID domain_id1cfrA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology91 — Restriction Endonuclease
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)