3cl3

Crystal Structure of a vFLIP-IKKgamma complex: Insights into viral activation of the IKK signalosome

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

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

ORF K13

Human gammaherpesvirus 8

UniProt P88961

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–178 Chain B; UniProt 1–178 Fragment:residues 1-178 NF-kappa-B essential modulator × 2 (Q9Y6K9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;225mM Tris pH 7.5, 4% Ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.20 Å R-free 0.287

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name P88961_HHV8
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–183; UniProt 1–178 Author chain B; PDBConstruct 6–183; UniProt 1–178

NF-kappa-B essential modulator

Homo sapiens

UniProt Q9Y6K9

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 150–272 Chain E; UniProt 150–272 Fragment:residues 150-272 ORF K13 × 2 (P88961) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;225mM Tris pH 7.5, 4% Ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.20 Å R-free 0.287

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.

11 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEMO_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 8–110; UniProt 150–272 Author chain E; PDBConstruct 8–110; UniProt 150–272

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 3cl3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3cl3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3cl3
Deposition date deposition_date2008-03-18
Structure title titleCrystal Structure of a vFLIP-IKKgamma complex: Insights into viral activation of the IKK signalosome
Keywords keywords;Death effector domain, coiled-coil, Coiled coil, Cytoplasm, Disease mutation, Ectodermal dysplasia, Host-virus interaction, Nucleus, Transcription, Transcription regulation, viral protein-signaling protein COMPLEX ;; viral protein/signaling protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.24
Radius of gyration Rg (electron density) rg_electron30.75
Forward intensity I(0) i041094700.00
Molecular weight molecular_weight49461.0 kDa
Excluded volume excluded_volume61761 ų
Envelope volume envelope_volume83357 ų
Hydration-shell volume shell_volume25591 ų
Envelope diameter envelope_diameter108.8
Shell Rg shell_rg33.22
Envelope Rg envelope_rg31.35
Shape Rg shape_rg30.69
Total Rg total_rg31.22
Total atoms total_atoms3477
Residues n_residues454
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_real31.45
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real4.1090e+07
I(0) uncertainty (real space) i0_real_error6.6430e+05
Rg (reciprocal space) rg_reciprocal31.37
I(0) (reciprocal space) i0_reciprocal41090000.0000
Solution quality estimate total_estimate0.6357
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.388
Kurtosis Kurtosis kurtosis-0.615
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha6702000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 0.040; Positv: 1.000; Valcen: 0.698; Smooth: 0.921

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3cl3A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology533 — Death Domain, Fas
Homologous superfamily homologous superfamily10 — Death Domain, Fas
Domain ID domain_id3cl3A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology533 — Death Domain, Fas
Homologous superfamily homologous superfamily10 — Death Domain, Fas
Domain ID domain_id3cl3B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology533 — Death Domain, Fas
Homologous superfamily homologous superfamily10 — Death Domain, Fas
Domain ID domain_id3cl3B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology533 — Death Domain, Fas
Homologous superfamily homologous superfamily10 — Death Domain, Fas
Domain ID domain_id3cl3D00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily390 — L1 transposable element, trimerization domain
Domain ID domain_id3cl3E00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily390 — L1 transposable element, trimerization domain

8. Citations (1)

9. Files and Curves (10)