3dqv

Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation

Method: X-RAY DIFFRACTION Dmax: 136.2 Å Quality: GOOD

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

NEDD8

Homo sapiens

UniProt Q15843

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 1–76 Fragment:NEDD8 C-terminus covalently linked to Cul5 Lys724 Mutation:L162M Non-standard monomer:Yes (specific site not provided by mmCIF) Cullin-5 × 1 (Q93034) Rbx1 × 1 (P62877) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–76 Fragment:NEDD8 C-terminus covalently linked to Cul5 Lys724 Mutation:L162M Non-standard monomer:Yes (specific site not provided by mmCIF) Cullin-5 × 1 (Q93034) Rbx1 × 1 (P62877) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299
3 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–76 Chain B; UniProt 1–76 Fragment:NEDD8 C-terminus covalently linked to Cul5 Lys724 Mutation:L162M Non-standard monomer:Yes (specific site not provided by mmCIF) Cullin-5 × 2 (Q93034) Rbx1 × 2 (P62877) ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299

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.

46 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEDD8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–81; UniProt 1–76 Author chain B; PDBConstruct 6–81; UniProt 1–76

Cullin-5

Homo sapiens

UniProt Q93034

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 401–780 Fragment:Cullin-5 residues 401-780 Mutation:L407E, L439K, V440K Non-standard monomer:Yes (specific site not provided by mmCIF) NEDD8 × 1 (Q15843) Rbx1 × 1 (P62877) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 401–780 Fragment:Cullin-5 residues 401-780 Mutation:L407E, L439K, V440K Non-standard monomer:Yes (specific site not provided by mmCIF) NEDD8 × 1 (Q15843) Rbx1 × 1 (P62877) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299
3 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 401–780 Chain D; UniProt 401–780 Fragment:Cullin-5 residues 401-780 Mutation:L407E, L439K, V440K Non-standard monomer:Yes (specific site not provided by mmCIF) NEDD8 × 2 (Q15843) Rbx1 × 2 (P62877) ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299

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.

13 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 3–382; UniProt 401–780 Author chain D; PDBConstruct 3–382; UniProt 401–780

Rbx1

Homo sapiens

UniProt P62877

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 R; UniProt 5–108 Fragment:Rbx1 residues 5-108 Non-standard monomer:Yes (specific site not provided by mmCIF) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Y; UniProt 5–108 Fragment:Rbx1 residues 5-108 Non-standard monomer:Yes (specific site not provided by mmCIF) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299
3 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 5–108 Chain Y; UniProt 5–108 Fragment:Rbx1 residues 5-108 Non-standard monomer:Yes (specific site not provided by mmCIF) NEDD8 × 2 (Q15843) Cullin-5 × 2 (Q93034) ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:277 K;with ~19% PEG3350, 275mM (NH4)2PO4, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.299

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.

99 other PDB entries and 105 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain R; PDBConstruct 3–106; UniProt 5–108 Author chain Y; PDBConstruct 3–106; UniProt 5–108

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 3dqv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3dqv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3dqv
Deposition date deposition_date2008-07-09
Structure title titleStructural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation
Keywords keywords;ubiquitin, nedd8, scf, cullin-ring ligase, cullin, Nucleus, Ubl conjugation pathway, Host-virus interaction, Receptor, Ubl conjugation, Acetylation, Cytoplasm, DNA damage, DNA repair, Metal-binding, Zinc, Zinc-finger, SIGNALING PROTEIN, LIGASE ;; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.73
Radius of gyration Rg (electron density) rg_electron39.09
Forward intensity I(0) i0253542000.00
Molecular weight molecular_weight127790.0 kDa
Excluded volume excluded_volume159320 ų
Envelope volume envelope_volume231910 ų
Hydration-shell volume shell_volume51061 ų
Envelope diameter envelope_diameter139.7
Shell Rg shell_rg43.02
Envelope Rg envelope_rg38.58
Shape Rg shape_rg39.09
Total Rg total_rg39.34
Total atoms total_atoms8839
Residues n_residues1046
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 dmax136.2
Rg (real space) rg_real39.74
Rg uncertainty (real space) rg_real_error1.84
I(0) (real space) i0_real2.5350e+08
I(0) uncertainty (real space) i0_real_error4.8280e+06
Rg (reciprocal space) rg_reciprocal39.73
I(0) (reciprocal space) i0_reciprocal253500000.0000
Solution quality estimate total_estimate0.8741
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.330
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14200000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd3dqva2
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_idd3dqva3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3dqvb1
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_idd3dqvb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3dqvr_
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.1 — RING finger domain, C3HC4
Domain ID domain_idd3dqvy_
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.1 — RING finger domain, C3HC4

CATH v4.4 (10 domains)

Domain ID domain_id3dqvA00
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
Domain ID domain_id3dqvB00
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
Domain ID domain_id3dqvC01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id3dqvC02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily130 — Cullin; Chain C, Domain 2
Domain ID domain_id3dqvC03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id3dqvD01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id3dqvD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily130 — Cullin; Chain C, Domain 2
Domain ID domain_id3dqvD03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id3dqvR00
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_id3dqvY00
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)

8. Citations (1)

9. Files and Curves (10)