5xiu

Crystal structure of RNF168 UDM2 in complex with Lys63-linked diubiquitin

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

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

E3 ubiquitin-protein ligase RNF168

Homo sapiens

UniProt Q8IYW5

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 419–462 Fragment:UNP residues 419-462 Ubiquitin-40S ribosomal protein S27a × 1 (P62983) EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;25% PEG3350, 0.1 M Tris-HCl (pH8.5), 0.2 M Ammonium Acetate Resolution 1.80 Å R-free 0.207

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.

38 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RN168_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–49; UniProt 419–462

Ubiquitin-40S ribosomal protein S27a

Mus musculus

UniProt P62983

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 B; UniProt 1–76 Not recorded E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;25% PEG3350, 0.1 M Tris-HCl (pH8.5), 0.2 M Ammonium Acetate Resolution 1.80 Å R-free 0.207

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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS27A_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; 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 5xiu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5xiu
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5xiu
Deposition date deposition_date2017-04-27
Structure title titleCrystal structure of RNF168 UDM2 in complex with Lys63-linked diubiquitin
Keywords keywordsubiquitin, TRANSFERASE-RIBOSOMAL PROTEIN complex; TRANSFERASE/RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.97
Radius of gyration Rg (electron density) rg_electron17.27
Forward intensity I(0) i04024960.00
Molecular weight molecular_weight14326.0 kDa
Excluded volume excluded_volume18024 ų
Envelope volume envelope_volume21657 ų
Hydration-shell volume shell_volume11999 ų
Envelope diameter envelope_diameter69.8
Shell Rg shell_rg21.44
Envelope Rg envelope_rg18.18
Shape Rg shape_rg17.26
Total Rg total_rg18.11
Total atoms total_atoms1005
Residues n_residues120
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_real18.32
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real4.0250e+06
I(0) uncertainty (real space) i0_real_error5.5600e+04
Rg (reciprocal space) rg_reciprocal18.27
I(0) (reciprocal space) i0_reciprocal4025000.0000
Solution quality estimate total_estimate0.7189
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.861
Kurtosis Kurtosis kurtosis0.650
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha565300.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.281; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.533; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5xiub_
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)