3wtd

Structure of PAXX

Method: X-RAY DIFFRACTION Dmax: 71.3 Å Quality: GOOD

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

Uncharacterized protein C9orf142

Homo sapiens

UniProt Q9BUH6

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–166 Chain B; UniProt 1–166 Fragment:N-terminal domain, UNP RESIDUES 1-166 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;1.5M ammonium sulfate, 12%(v/v) glycerol, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.35 Å R-free 0.229

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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CI142_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–168; UniProt 1–166 Author chain B; PDBConstruct 3–168; UniProt 1–166

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 3wtd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3wtd
Deposition date deposition_date2014-04-09
Structure title titleStructure of PAXX
Keywords keywordsDNA repair, Scaffold, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.35
Radius of gyration Rg (electron density) rg_electron20.38
Forward intensity I(0) i013757600.00
Molecular weight molecular_weight27813.0 kDa
Excluded volume excluded_volume34878 ų
Envelope volume envelope_volume42836 ų
Hydration-shell volume shell_volume18368 ų
Envelope diameter envelope_diameter71.9
Shell Rg shell_rg25.90
Envelope Rg envelope_rg20.56
Shape Rg shape_rg20.40
Total Rg total_rg21.14
Total atoms total_atoms1958
Residues n_residues268
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 dmax71.3
Rg (real space) rg_real21.41
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.3760e+07
I(0) uncertainty (real space) i0_real_error1.8800e+05
Rg (reciprocal space) rg_reciprocal21.40
I(0) (reciprocal space) i0_reciprocal13760000.0000
Solution quality estimate total_estimate0.7991
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.448
Kurtosis Kurtosis kurtosis-0.169
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3267000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)