5um9

Flap endonuclease 1 (FEN1) D86N with 5'-flap substrate DNA and Sm3+

Method: X-RAY DIFFRACTION Dmax: 78.0 Å Quality: GOOD

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

Flap endonuclease 1

Homo sapiens

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–DNA Monomer Protein × 1 DNA 3 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 2–336 Mutation:D86N ;DNA (5'-D(*AP*CP*TP*CP*TP*GP*CP*CP*TP*CP*AP*AP*GP*AP*CP*GP*GP*T)-3') ; × 1 ;DNA (5'-D(P*TP*CP*TP*TP*GP*AP*GP*GP*CP*AP*GP*AP*GP*T)-3') ; × 1 ;DNA (5'-D(*AP*CP*CP*GP*TP*CP*C)-3') ; × 1 K POTASSIUM ION × 1 SM SAMARIUM (III) ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;283 K;6% MPEG 2K, 10% KCl, 50 mM HEPES pH 7.5, 2.5% Ethylene glycol, 1.06 mM SmSO4 Resolution 2.81 Å R-free 0.266

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 A; PDBConstruct 1–335; UniProt 2–336

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 5um9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5um9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5um9
Deposition date deposition_date2017-01-26
Structure title titleFlap endonuclease 1 (FEN1) D86N with 5'-flap substrate DNA and Sm3+
Keywords keywords;dna repair, endonuclease, 5' nuclease, DNA binding, 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_guinier24.47
Radius of gyration Rg (electron density) rg_electron23.38
Forward intensity I(0) i059335100.00
Molecular weight molecular_weight51143.0 kDa
Excluded volume excluded_volume60090 ų
Envelope volume envelope_volume77309 ų
Hydration-shell volume shell_volume27485 ų
Envelope diameter envelope_diameter81.8
Shell Rg shell_rg30.59
Envelope Rg envelope_rg23.58
Shape Rg shape_rg23.33
Total Rg total_rg24.25
Total atoms total_atoms6666
Residues n_residues380
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 dmax78.0
Rg (real space) rg_real24.42
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real5.9340e+07
I(0) uncertainty (real space) i0_real_error7.6350e+05
Rg (reciprocal space) rg_reciprocal24.43
I(0) (reciprocal space) i0_reciprocal59340000.0000
Solution quality estimate total_estimate0.8966
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.328
Kurtosis Kurtosis kurtosis-0.297
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7471000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5um9A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1010 — 5'-nuclease
Domain ID domain_id5um9A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily20 — 5' to 3' exonuclease, C-terminal subdomain

8. Citations (1)

9. Files and Curves (10)