4xok

Observing the overall rocking motion of a protein in a crystal.

Method: X-RAY DIFFRACTION Dmax: 79.3 Å Quality: REASONABLE

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

Ubiquitin

Homo sapiens

UniProt P0CG48

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 1–76 Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;20mg/ml Ubi in 20mM NH4Ac pH4.3, 50mM HEPES pH7.0, 35% PEG 1500, 25mM Zn Acetate Resolution 2.20 Å R-free 0.324
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–76 Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;20mg/ml Ubi in 20mM NH4Ac pH4.3, 50mM HEPES pH7.0, 35% PEG 1500, 25mM Zn Acetate Resolution 2.20 Å R-free 0.324
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–76 Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;20mg/ml Ubi in 20mM NH4Ac pH4.3, 50mM HEPES pH7.0, 35% PEG 1500, 25mM Zn Acetate Resolution 2.20 Å R-free 0.324

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.

219 other PDB entries and 346 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 1–76 Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain C; 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 4xok

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4xok
Deposition date deposition_date2015-01-16
Structure title titleObserving the overall rocking motion of a protein in a crystal.
Keywords keywordsubiquitin, Zinc, signaling protein; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.73
Radius of gyration Rg (electron density) rg_electron22.18
Forward intensity I(0) i010794000.00
Molecular weight molecular_weight24612.0 kDa
Excluded volume excluded_volume30846 ų
Envelope volume envelope_volume37972 ų
Hydration-shell volume shell_volume15809 ų
Envelope diameter envelope_diameter72.3
Shell Rg shell_rg26.84
Envelope Rg envelope_rg22.03
Shape Rg shape_rg22.19
Total Rg total_rg22.81
Total atoms total_atoms1709
Residues n_residues214
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 dmax79.3
Rg (real space) rg_real22.90
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real1.0790e+07
I(0) uncertainty (real space) i0_real_error1.6680e+05
Rg (reciprocal space) rg_reciprocal22.86
I(0) (reciprocal space) i0_reciprocal10790000.0000
Solution quality estimate total_estimate0.7176
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.2
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis-0.526
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9268000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.570; Stabil: 0.993; Sysdev: 1.000; Positv: 1.000; Valcen: 0.636; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4xoka_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd4xokb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd4xokc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related

8. Citations (1)

9. Files and Curves (10)