9bj9

Human CRL-2 ZYG11B binding to human NLRP1 Gly/N degron

Method: ELECTRON MICROSCOPY Dmax: 160.7 Å Quality: GOOD

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

Protein zyg-11 homolog B

Homo sapiens

UniProt Q9C0D3

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 2–744 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Cullin-2 × 1 (Q13617) Peptide from NACHT, LRR and PYD domains-containing protein 1, N-terminus × 1 (Q9C000) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ZY11B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–748; UniProt 2–744

Elongin-B

Homo sapiens

UniProt Q15370

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–118 Not recorded Protein zyg-11 homolog B × 1 (Q9C0D3) Elongin-C × 1 (Q15369) Cullin-2 × 1 (Q13617) Peptide from NACHT, LRR and PYD domains-containing protein 1, N-terminus × 1 (Q9C000) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–118; UniProt 1–118

Elongin-C

Homo sapiens

UniProt Q15369

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 17–112 Not recorded Protein zyg-11 homolog B × 1 (Q9C0D3) Elongin-B × 1 (Q15370) Cullin-2 × 1 (Q13617) Peptide from NACHT, LRR and PYD domains-containing protein 1, N-terminus × 1 (Q9C000) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–96; UniProt 17–112

Cullin-2

Homo sapiens

UniProt Q13617

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–745 Not recorded Protein zyg-11 homolog B × 1 (Q9C0D3) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Peptide from NACHT, LRR and PYD domains-containing protein 1, N-terminus × 1 (Q9C000) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

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.

41 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–745; UniProt 1–745

Peptide from NACHT, LRR and PYD domains-containing protein 1, N-terminus

Homo sapiens

UniProt Q9C000

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain P; UniProt 131–139 Fragment:residues 131-139 (Uniprot numbering) Protein zyg-11 homolog B × 1 (Q9C0D3) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Cullin-2 × 1 (Q13617) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

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 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NLRP1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 1–9; UniProt 131–139

E3 ubiquitin-protein ligase 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 1–108 Not recorded Protein zyg-11 homolog B × 1 (Q9C0D3) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Cullin-2 × 1 (Q13617) Peptide from NACHT, LRR and PYD domains-containing protein 1, N-terminus × 1 (Q9C000) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

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 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain R; PDBConstruct 1–108; UniProt 1–108

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 9bj9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bj9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bj9
Deposition date deposition_date2024-04-25
Structure title titleHuman CRL-2 ZYG11B binding to human NLRP1 Gly/N degron
Keywords keywordsGly/N degron, Cullin E3 ligase, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.00
Radius of gyration Rg (electron density) rg_electron53.71
Forward intensity I(0) i0587403000.00
Molecular weight molecular_weight202500.0 kDa
Excluded volume excluded_volume253810 ų
Envelope volume envelope_volume425380 ų
Hydration-shell volume shell_volume67152 ų
Envelope diameter envelope_diameter170.9
Shell Rg shell_rg57.90
Envelope Rg envelope_rg50.71
Shape Rg shape_rg53.72
Total Rg total_rg53.83
Total atoms total_atoms14204
Residues n_residues1767
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 dmax160.7
Rg (real space) rg_real53.99
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real5.8740e+08
I(0) uncertainty (real space) i0_real_error1.0790e+07
Rg (reciprocal space) rg_reciprocal53.98
I(0) (reciprocal space) i0_reciprocal587400000.0000
Solution quality estimate total_estimate0.8438
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.0
Skewness Skewness skewness0.144
Kurtosis Kurtosis kurtosis-0.745
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25360000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.988; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.011

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (2)

9. Files and Curves (10)