5x3o

Crystal structure of p-DiUb-S65-COOH

Method: X-RAY DIFFRACTION Dmax: 59.0 Å Quality: GOOD

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

Polyubiquitin-B

Homo sapiens

UniProt P0CG47

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–76 Fragment:UNP residues 1-76 Non-standard monomer:Yes (specific site not provided by mmCIF) D-ubiquitin × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.2M Ammonium phosphate monobasic, 20%(w/v) Polyethylene glycol 3350 Resolution 2.19 Å R-free 0.315

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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 1–76

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 5x3o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5x3o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5x3o
Deposition date deposition_date2017-02-06
Structure title titleCrystal structure of p-DiUb-S65-COOH
Keywords keywordsUbiquitin, Synthesis, phosphorylation, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.30
Radius of gyration Rg (electron density) rg_electron17.49
Forward intensity I(0) i05003150.00
Molecular weight molecular_weight16946.0 kDa
Excluded volume excluded_volume21719 ų
Envelope volume envelope_volume25285 ų
Hydration-shell volume shell_volume12908 ų
Envelope diameter envelope_diameter59.6
Shell Rg shell_rg21.99
Envelope Rg envelope_rg17.43
Shape Rg shape_rg17.46
Total Rg total_rg18.41
Total atoms total_atoms1186
Residues n_residues78
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 dmax59.0
Rg (real space) rg_real18.33
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real5.0030e+06
I(0) uncertainty (real space) i0_real_error6.0400e+04
Rg (reciprocal space) rg_reciprocal18.32
I(0) (reciprocal space) i0_reciprocal5003000.0000
Solution quality estimate total_estimate0.8795
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.355
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1266000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)