1rw2

Three-dimensional structure of Ku80 CTD

Method: SOLUTION NMR Dmax: 63.2 Å Quality: REASONABLE

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

ATP-dependent DNA helicase II, 80 kDa subunit

Homo sapiens

UniProt P13010

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 565–709 Fragment:Ku80 C-terminal Domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 100 mM phosphate buffer;Pressure 1 NMR sample composition:Approximately 1 mM N-15/C-13 labeled protein in 100 mM phosphate buffer, pH 6.0, and 5 mM DTT | 100% D2O NMR sample composition:Approximately 1 mM N-15/C-13 labeled protein in 100 mM phosphate buffer, pH 6.0, and 5 mM DTT | 90% H2O/10% D2O NMR sample composition:Approximately 1 mM N-15 labeled protein in 100 mM phosphate buffer, pH 6.0, an | 90% H2O/10% D2O Resolution not provided

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.

62 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KU86_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–152; UniProt 565–709

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 1rw2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rw2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rw2
Deposition date deposition_date2003-12-15
Structure title titleThree-dimensional structure of Ku80 CTD
Keywords keywordsKu80, NHEJ, DNA-PK, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier23.15
Radius of gyration Rg (electron density) rg_electron22.85
Forward intensity I(0) i0438895000.00
Molecular weight molecular_weight173210.0 kDa
Excluded volume excluded_volume216190 ų
Envelope volume envelope_volume120570 ų
Hydration-shell volume shell_volume31230 ų
Envelope diameter envelope_diameter139.8
Shell Rg shell_rg36.90
Envelope Rg envelope_rg38.26
Shape Rg shape_rg22.86
Total Rg total_rg23.38
Total atoms total_atoms24330
Residues n_residues1520
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 dmax63.2
Rg (real space) rg_real20.31
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real4.1360e+08
I(0) uncertainty (real space) i0_real_error4.2300e+06
Rg (reciprocal space) rg_reciprocal24.00
I(0) (reciprocal space) i0_reciprocal438800000.0000
Solution quality estimate total_estimate0.6119
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.690
Kurtosis Kurtosis kurtosis-0.124
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha1.2500
Highest regularization parameter α highest_alpha1274000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.013; Oscil: 0.741; Stabil: 0.989; Sysdev: 0.000; Positv: 1.000; Valcen: 0.836; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1rw2a1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.19 — C-terminal domain of Ku80
Family Family familya.118.19.1 — C-terminal domain of Ku80
Domain ID domain_idd1rw2a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1rw2A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily240 — Ku, C-terminal domain

8. Citations (1)

9. Files and Curves (10)