3jsv

Crystal structure of mouse NEMO CoZi in complex with Lys63-linked di-ubiquitin

Method: X-RAY DIFFRACTION Dmax: 133.3 Å Quality: REASONABLE

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

Ubiquitin

Homo sapiens

UniProt P62988

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 1–76 Chain B; UniProt 1–76 Mutation:K63R Mutation:X77D NF-kappa-B essential modulator × 2 (O88522) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.70 Å R-free 0.294

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.

83 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBIQ_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 1–76 Author chain B; PDBConstruct 1–76; UniProt 1–76

NF-kappa-B essential modulator

Mus musculus

UniProt O88522

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 C; UniProt 250–343 Chain D; UniProt 250–343 Fragment:residues 250-343 Ubiquitin × 1 (P62988) Ubiquitin × 1 (P62988) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.70 Å R-free 0.294

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEMO_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–94; UniProt 250–343 Author chain D; PDBConstruct 1–94; UniProt 250–343

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 3jsv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3jsv
Deposition date deposition_date2009-09-11
Structure title titleCrystal structure of mouse NEMO CoZi in complex with Lys63-linked di-ubiquitin
Keywords keywords;ubiquitin, coiled-coil, cellular signaling, Cytoplasm, Isopeptide bond, Nucleus, Phosphoprotein, Ubl conjugation, Coiled coil, Disulfide bond, Metal-binding, Transcription, Transcription regulation, Zinc, Zinc-finger, SIGNALING PROTEIN-TRANSCRIPTION COMPLEX ;; SIGNALING PROTEIN/TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.01
Radius of gyration Rg (electron density) rg_electron33.89
Forward intensity I(0) i023167600.00
Molecular weight molecular_weight37328.0 kDa
Excluded volume excluded_volume46905 ų
Envelope volume envelope_volume67636 ų
Hydration-shell volume shell_volume20256 ų
Envelope diameter envelope_diameter140.1
Shell Rg shell_rg32.85
Envelope Rg envelope_rg35.57
Shape Rg shape_rg33.87
Total Rg total_rg33.86
Total atoms total_atoms2626
Residues n_residues322
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 dmax133.3
Rg (real space) rg_real34.13
Rg uncertainty (real space) rg_real_error1.93
I(0) (real space) i0_real2.3170e+07
I(0) uncertainty (real space) i0_real_error4.3900e+05
Rg (reciprocal space) rg_reciprocal33.65
I(0) (reciprocal space) i0_reciprocal23160000.0000
Solution quality estimate total_estimate0.6885
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.6
Skewness Skewness skewness0.871
Kurtosis Kurtosis kurtosis0.352
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1589000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.322; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.091; Smooth: 0.890

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3jsva_
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_idd3jsvb_
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_id3jsvA00
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_id3jsvB00
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_id3jsvC00
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 superfamily990 — Nemo cc2-lz domain - 1d5 darpin complex
Domain ID domain_id3jsvD00
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 superfamily990 — Nemo cc2-lz domain - 1d5 darpin complex

8. Citations (1)

9. Files and Curves (10)