5d0k

Structure of UbE2D2:RNF165:Ub complex

Method: X-RAY DIFFRACTION Dmax: 160.5 Å Quality: REASONABLE

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

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–147 Mutation:C21S, C85K, C107S, C111S RING finger protein 165 × 1 (Q6ZSG1) Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–147 Mutation:C21S, C85K, C107S, C111S RING finger protein 165 × 1 (Q6ZSG1) Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–147 Mutation:C21S, C85K, C107S, C111S RING finger protein 165 × 1 (Q6ZSG1) Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 1–147 Mutation:C21S, C85K, C107S, C111S RING finger protein 165 × 1 (Q6ZSG1) Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238

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 89 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–152; UniProt 1–147 Author chain D; PDBConstruct 6–152; UniProt 1–147 Author chain G; PDBConstruct 6–152; UniProt 1–147 Author chain J; PDBConstruct 6–152; UniProt 1–147

RING finger protein 165

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 255–346 Fragment:UNP residues 255-346 Mutation:del273-277 Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 255–346 Fragment:UNP residues 255-346 Mutation:del273-277 Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 255–346 Fragment:UNP residues 255-346 Mutation:del273-277 Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 255–346 Fragment:UNP residues 255-346 Mutation:del273-277 Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RN165_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 6–92; UniProt 255–346 Author chain F; PDBConstruct 6–92; UniProt 255–346 Author chain I; PDBConstruct 6–92; UniProt 255–346 Author chain L; PDBConstruct 6–92; UniProt 255–346

Polyubiquitin-B

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–76 Fragment:UNP residues 1-76 Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) RING finger protein 165 × 1 (Q6ZSG1) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–76 Fragment:UNP residues 1-76 Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) RING finger protein 165 × 1 (Q6ZSG1) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 1–76 Fragment:UNP residues 1-76 Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) RING finger protein 165 × 1 (Q6ZSG1) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 1–76 Fragment:UNP residues 1-76 Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) RING finger protein 165 × 1 (Q6ZSG1) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.15 K;MES, sodium chloride, PEG 6000 Resolution 2.65 Å R-free 0.238

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 426 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain E; PDBConstruct 1–76; UniProt 1–76 Author chain H; PDBConstruct 1–76; UniProt 1–76 Author chain K; 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 5d0k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5d0k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5d0k
Deposition date deposition_date2015-08-03
Structure title titleStructure of UbE2D2:RNF165:Ub complex
Keywords keywordscomplex, ubiquitin, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier47.64
Radius of gyration Rg (electron density) rg_electron48.29
Forward intensity I(0) i0261068000.00
Molecular weight molecular_weight133590.0 kDa
Excluded volume excluded_volume167550 ų
Envelope volume envelope_volume241390 ų
Hydration-shell volume shell_volume45721 ų
Envelope diameter envelope_diameter170.8
Shell Rg shell_rg45.94
Envelope Rg envelope_rg47.80
Shape Rg shape_rg48.32
Total Rg total_rg48.12
Total atoms total_atoms9359
Residues n_residues1169
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 dmax160.5
Rg (real space) rg_real49.74
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real2.6080e+08
I(0) uncertainty (real space) i0_real_error4.0290e+06
Rg (reciprocal space) rg_reciprocal47.65
I(0) (reciprocal space) i0_reciprocal260800000.0000
Solution quality estimate total_estimate0.6193
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.8
Skewness Skewness skewness0.526
Kurtosis Kurtosis kurtosis-0.518
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha1.7520
Highest regularization parameter α highest_alpha12620000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.756; Stabil: 0.932; Sysdev: 0.000; Positv: 1.000; Valcen: 0.804; Smooth: 0.187

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd5d0ka1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd5d0ka2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5d0kb_
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_idd5d0kd1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd5d0kd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5d0ke_
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_idd5d0kg1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd5d0kg2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5d0kh_
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_idd5d0kj1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd5d0kj2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5d0kk_
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

CATH v4.4 (4 domains)

Domain ID domain_id5d0kA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme
Domain ID domain_id5d0kD00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme
Domain ID domain_id5d0kG00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme
Domain ID domain_id5d0kJ00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme

8. Citations (1)

9. Files and Curves (10)