1q2z

The 3D solution structure of the C-terminal region of Ku86

Method: SOLUTION NMR Dmax: 52.2 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 591–708 Fragment:Ku86CTR (591-709) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 100 mM NaCl;Pressure ambient NMR measurement conditions:pH 7;293 K;Ionic strength (raw mmCIF value) 100 mM NaCl;Pressure ambient NMR sample composition:1mM U-15N; 20mM Phosphate; 100mM NaCl; 1mM NaN3 | 90% H2O/10% D2O NMR sample composition:1mM U-13C,15N; 20mM Phosphate; 100mM NaCl; 1mM NaN3 | 90% H2O/10% D2O NMR sample composition:1mM U-15N; 20mM Phosphate; 100mM NaCl; 1mM NaN3; 5% n-octyl-penta(ethylene glycol):octanol 0.96:1 | 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 1–120; UniProt 591–708

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 1q2z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1q2z
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1q2z
Deposition date deposition_date2003-07-28
Structure title titleThe 3D solution structure of the C-terminal region of Ku86
Keywords keywordsKu, DNA repair, protein structure, NMR spectroscopy, DNA-PK, Ku86, Ku80, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.17
Radius of gyration Rg (electron density) rg_electron14.88
Forward intensity I(0) i01020130000.00
Molecular weight molecular_weight276570.0 kDa
Excluded volume excluded_volume348140 ų
Envelope volume envelope_volume33781 ų
Hydration-shell volume shell_volume16639 ų
Envelope diameter envelope_diameter60.2
Shell Rg shell_rg23.25
Envelope Rg envelope_rg17.50
Shape Rg shape_rg14.83
Total Rg total_rg15.20
Total atoms total_atoms38980
Residues n_residues2400
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 dmax52.2
Rg (real space) rg_real15.08
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.0200e+09
I(0) uncertainty (real space) i0_real_error1.2450e+07
Rg (reciprocal space) rg_reciprocal15.09
I(0) (reciprocal space) i0_reciprocal1020000000.0000
Solution quality estimate total_estimate0.6296
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.8
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.264
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha281300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.695; Stabil: 0.998; Sysdev: 0.368; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1q2za_
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

CATH v4.4 (1 domains)

Domain ID domain_id1q2zA00
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)