8f1f

Structure of K48-linked tri-ubiquitin in complex with cyclic peptide

Method: X-RAY DIFFRACTION Dmax: 103.5 Å Quality: GOOD

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

Ubiquitin

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–76 Chain B; UniProt 1–76 Chain C; UniProt 1–76 Mutation:D77 added to the C-terminus Mutation:K48R Non-proteinogenic cyclic peptide (inhibitor) × 1 GOL GLYCEROL × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Droplets were formed by mixing equal volumes of Ub3:Ub4a complex (8 mg/ml) and the crystallization solution containing 0.15 M NaCl, 23% (w/v) PEG 3350 and 0.1 M HEPES (pH 7.5) Resolution 1.85 Å R-free 0.298
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain a; UniProt 1–76 Chain b; UniProt 1–76 Chain c; UniProt 1–76 Mutation:D77 added to the C-terminus Mutation:K48R Non-proteinogenic cyclic peptide (inhibitor) × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Droplets were formed by mixing equal volumes of Ub3:Ub4a complex (8 mg/ml) and the crystallization solution containing 0.15 M NaCl, 23% (w/v) PEG 3350 and 0.1 M HEPES (pH 7.5) Resolution 1.85 Å R-free 0.298

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 428 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 1, 2, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 1–76 Author chain a; PDBConstruct 1–76; UniProt 1–76 Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain b; PDBConstruct 1–76; UniProt 1–76 Author chain C; 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 8f1f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8f1f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8f1f
Deposition date deposition_date2022-11-05
Structure title titleStructure of K48-linked tri-ubiquitin in complex with cyclic peptide
Keywords keywordscomplex, therapeutic peptide, Lys48-linked polyubiquitin, macrocyclic peptide, inhibitor of ubiquitin signaling, 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_guinier30.02
Radius of gyration Rg (electron density) rg_electron29.29
Forward intensity I(0) i047525300.00
Molecular weight molecular_weight54989.0 kDa
Excluded volume excluded_volume69522 ų
Envelope volume envelope_volume90422 ų
Hydration-shell volume shell_volume26936 ų
Envelope diameter envelope_diameter102.7
Shell Rg shell_rg34.87
Envelope Rg envelope_rg29.07
Shape Rg shape_rg29.30
Total Rg total_rg29.86
Total atoms total_atoms3864
Residues n_residues472
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 dmax103.5
Rg (real space) rg_real30.19
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real4.7530e+07
I(0) uncertainty (real space) i0_real_error7.7590e+05
Rg (reciprocal space) rg_reciprocal30.12
I(0) (reciprocal space) i0_reciprocal47520000.0000
Solution quality estimate total_estimate0.8587
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.2
Skewness Skewness skewness0.460
Kurtosis Kurtosis kurtosis-0.331
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11260000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.802; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.853; Smooth: 0.898

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)