5xit

Crystal structure of RNF168 UDM1 in complex with Lys63-linked diubiquitin, form II

Method: X-RAY DIFFRACTION Dmax: 103.8 Å Quality: REASONABLE

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–76 Chain D; UniProt 1–76 Mutation:K63R E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;23% PEG MME 2000, 0.1 M Bis-Tris (pH 6.5), 10 mM Pr acetate Resolution 2.25 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–76 Chain H; UniProt 1–76 Mutation:K63R E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) GOL GLYCEROL × 1 PR PRASEODYMIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;23% PEG MME 2000, 0.1 M Bis-Tris (pH 6.5), 10 mM Pr acetate Resolution 2.25 Å R-free 0.239

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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS27A_MOUSE
Isoform
PDB entities 1, 3
Chains and sequence ranges Author chain D; PDBConstruct 1–76; UniProt 1–76 Author chain F; PDBConstruct 1–76; UniProt 1–76 Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain H; PDBConstruct 1–76; UniProt 1–76

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 113–188 Fragment:UNP residues 113-188 Ubiquitin-40S ribosomal protein S27a × 1 (P62983) Ubiquitin-40S ribosomal protein S27a × 1 (P62983) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;23% PEG MME 2000, 0.1 M Bis-Tris (pH 6.5), 10 mM Pr acetate Resolution 2.25 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 113–188 Fragment:UNP residues 113-188 Ubiquitin-40S ribosomal protein S27a × 1 (P62983) Ubiquitin-40S ribosomal protein S27a × 1 (P62983) GOL GLYCEROL × 1 PR PRASEODYMIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;23% PEG MME 2000, 0.1 M Bis-Tris (pH 6.5), 10 mM Pr acetate Resolution 2.25 Å R-free 0.239

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 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RN168_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 6–81; UniProt 113–188 Author chain E; PDBConstruct 6–81; UniProt 113–188

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 5xit

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5xit
Deposition date deposition_date2017-04-27
Structure title titleCrystal structure of RNF168 UDM1 in complex with Lys63-linked diubiquitin, form II
Keywords keywordsprotein complex, DNA repair, 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_guinier38.06
Radius of gyration Rg (electron density) rg_electron39.19
Forward intensity I(0) i048207300.00
Molecular weight molecular_weight52823.0 kDa
Excluded volume excluded_volume65459 ų
Envelope volume envelope_volume98180 ų
Hydration-shell volume shell_volume25264 ų
Envelope diameter envelope_diameter197.6
Shell Rg shell_rg36.06
Envelope Rg envelope_rg41.73
Shape Rg shape_rg39.18
Total Rg total_rg38.95
Total atoms total_atoms3682
Residues n_residues450
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 dmax103.8
Rg (real space) rg_real34.51
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real4.5800e+07
I(0) uncertainty (real space) i0_real_error6.6190e+05
Rg (reciprocal space) rg_reciprocal38.55
I(0) (reciprocal space) i0_reciprocal48160000.0000
Solution quality estimate total_estimate0.6747
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.0
Skewness Skewness skewness0.418
Kurtosis Kurtosis kurtosis-0.413
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.7569
Highest regularization parameter α highest_alpha2173000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.011; Oscil: 0.973; Stabil: 0.977; Sysdev: 0.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5xitb_
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_idd5xitd_
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_idd5xitf_
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_idd5xith_
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)