4rec

A nuclease-DNA complex form 3

Method: X-RAY DIFFRACTION Dmax: 101.1 Å Quality: GOOD

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

Fanconi-associated nuclease 1

Homo sapiens

UniProt Q9Y2M0

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 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 373–1017 Fragment:UNP residues 373-1017 Mutation:D960A DNA (40-MER) × 1 IOD IODIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:micro-batch under oil;300 K;0.1M potassium iodide, 0.1mM spermidine, 18% PEG3350, 0.1M BisTris propane, micro-batch under oil, temperature 300K Resolution 2.20 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.

17 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FAN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–647; UniProt 373–1017

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 4rec

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4rec
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4rec
Deposition date deposition_date2014-09-22
Structure title titleA nuclease-DNA complex form 3
Keywords keywordsHJC, TPR, SAP, structure specific nuclease, FANCID2, nucleus, 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_guinier31.81
Radius of gyration Rg (electron density) rg_electron30.63
Forward intensity I(0) i0125551000.00
Molecular weight molecular_weight80488.0 kDa
Excluded volume excluded_volume97251 ų
Envelope volume envelope_volume135200 ų
Hydration-shell volume shell_volume37650 ų
Envelope diameter envelope_diameter107.7
Shell Rg shell_rg37.02
Envelope Rg envelope_rg30.09
Shape Rg shape_rg30.59
Total Rg total_rg31.29
Total atoms total_atoms5595
Residues n_residues633
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 dmax101.1
Rg (real space) rg_real31.75
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.2560e+08
I(0) uncertainty (real space) i0_real_error2.1360e+06
Rg (reciprocal space) rg_reciprocal31.78
I(0) (reciprocal space) i0_reciprocal125600000.0000
Solution quality estimate total_estimate0.8993
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.4
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.372
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8465000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.872

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)