3uvu

Structural basis of nuclear import of Flap endonuclease 1 (FEN1)

Method: X-RAY DIFFRACTION Dmax: 97.1 Å Quality: GOOD

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

Flap endonuclease 1 (Fen1) peptide

OrganismNot specified

UniProt P39748

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 352–370 Not recorded Importin subunit alpha-2 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.8;293 K;Sodium citrate, DTT, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.38 Å R-free 0.215

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.

26 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FEN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–19; UniProt 352–370

Importin subunit alpha-2

Mus musculus

UniProt P52293

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 70–529 Not recorded Flap endonuclease 1 (Fen1) peptide × 1 (P39748) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.8;293 K;Sodium citrate, DTT, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.38 Å R-free 0.215

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.

150 other PDB entries and 151 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMA2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 51–510; UniProt 70–529

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 3uvu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3uvu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3uvu
Deposition date deposition_date2011-11-30
Structure title titleStructural basis of nuclear import of Flap endonuclease 1 (FEN1)
Keywords keywordsFen 1, Flap Endonuclease 1, PROTEIN BINDING-PEPTIDE complex; PROTEIN BINDING/PEPTIDE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.63
Radius of gyration Rg (electron density) rg_electron27.41
Forward intensity I(0) i034663900.00
Molecular weight molecular_weight47152.0 kDa
Excluded volume excluded_volume59694 ų
Envelope volume envelope_volume70792 ų
Hydration-shell volume shell_volume23373 ų
Envelope diameter envelope_diameter99.2
Shell Rg shell_rg32.14
Envelope Rg envelope_rg27.56
Shape Rg shape_rg27.42
Total Rg total_rg27.88
Total atoms total_atoms3320
Residues n_residues444
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 dmax97.1
Rg (real space) rg_real27.97
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real3.4660e+07
I(0) uncertainty (real space) i0_real_error5.1000e+05
Rg (reciprocal space) rg_reciprocal27.87
I(0) (reciprocal space) i0_reciprocal34660000.0000
Solution quality estimate total_estimate0.7979
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.561
Kurtosis Kurtosis kurtosis-0.337
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14960000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.630; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.574; Smooth: 0.905

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3uvuA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)