7r71

Crystal Structure of the UbArk2C-UbcH5b~Ub complex

Method: X-RAY DIFFRACTION Dmax: 80.0 Å Quality: REASONABLE

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

Ubiquitin,E3 ubiquitin-protein ligase RNF165

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 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–76 Chain D; UniProt 1–76 Not recorded Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.1 M MMT pH 6.0, 25% w/v PEG 1500 Resolution 2.80 Å R-free 0.271

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 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 6–81; UniProt 1–76 Author chain D; PDBConstruct 1–76; UniProt 1–76

Ubiquitin,E3 ubiquitin-protein ligase RNF165

Homo sapiens

UniProt Q6ZSG1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 255–346 Not recorded Ubiquitin × 1 (P0CG48) Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.1 M MMT pH 6.0, 25% w/v PEG 1500 Resolution 2.80 Å R-free 0.271

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.

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

View Construct and Data Evidence
UniProt name RN165_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 92–183; UniProt 255–346

Ubiquitin-conjugating enzyme E2 D2

Homo sapiens

UniProt P62837

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–147 Mutation:C21S, S22R, C85K, C107S, C111S Ubiquitin,E3 ubiquitin-protein ligase RNF165 × 1 (P0CG48,Q6ZSG1) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.1 M MMT pH 6.0, 25% w/v PEG 1500 Resolution 2.80 Å R-free 0.271

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.

57 other PDB entries and 92 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–152; UniProt 1–147

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 7r71

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7r71
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7r71
Deposition date deposition_date2021-06-24
Structure title titleCrystal Structure of the UbArk2C-UbcH5b~Ub complex
Keywords keywordsRING E3 ligase Ubiquitin PTM, LIGASE, E2~Ub conjugate, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.87
Radius of gyration Rg (electron density) rg_electron22.90
Forward intensity I(0) i030257100.00
Molecular weight molecular_weight42334.0 kDa
Excluded volume excluded_volume53159 ų
Envelope volume envelope_volume64735 ų
Hydration-shell volume shell_volume24187 ų
Envelope diameter envelope_diameter81.7
Shell Rg shell_rg29.52
Envelope Rg envelope_rg23.03
Shape Rg shape_rg22.93
Total Rg total_rg23.65
Total atoms total_atoms2969
Residues n_residues369
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 dmax80.0
Rg (real space) rg_real23.90
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real3.0260e+07
I(0) uncertainty (real space) i0_real_error4.2460e+05
Rg (reciprocal space) rg_reciprocal23.89
I(0) (reciprocal space) i0_reciprocal30260000.0000
Solution quality estimate total_estimate0.6850
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.404
Kurtosis Kurtosis kurtosis-0.246
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha9950000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 0.154; Positv: 1.000; Valcen: 0.970; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7r71A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id7r71C01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme
Domain ID domain_id7r71D01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)