9nr3

CRBN-DDB1 in complex with GLUL-cN

Method: X-RAY DIFFRACTION Dmax: 108.8 Å Quality: GOOD

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

DNA damage-binding protein 1

Homo sapiens

UniProt Q16531

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 1–393 Chain A; UniProt 709–1140 Not recorded Protein cereblon × 1 (Q96SW2) GLUL-cN × 1 (P15104) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;8% v/v TacsimateTM pH 6.0, 20% w/v Polyethylene glycol 3,350 Resolution 2.93 Å R-free 0.278

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.

202 other PDB entries and 290 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–393; UniProt 1–393 Author chain A; PDBConstruct 395–826; UniProt 709–1140

Protein cereblon

Homo sapiens

UniProt Q96SW2

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 41–442 Not recorded DNA damage-binding protein 1 × 1 (Q16531) GLUL-cN × 1 (P15104) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;8% v/v TacsimateTM pH 6.0, 20% w/v Polyethylene glycol 3,350 Resolution 2.93 Å R-free 0.278

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.

93 other PDB entries and 141 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRBN_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–402; UniProt 41–442

GLUL-cN

OrganismNot specified

UniProt P15104

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 D; UniProt 368–373 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;8% v/v TacsimateTM pH 6.0, 20% w/v Polyethylene glycol 3,350 Resolution 2.93 Å R-free 0.278

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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLNA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–6; UniProt 368–373

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 9nr3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9nr3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9nr3
Deposition date deposition_date2025-03-13
Structure title titleCRBN-DDB1 in complex with GLUL-cN
Keywords keywordsubiquitin ligase, native substrate, degron, glutamine synthetase, CRBN, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.05
Radius of gyration Rg (electron density) rg_electron33.16
Forward intensity I(0) i0255902000.00
Molecular weight molecular_weight129450.0 kDa
Excluded volume excluded_volume162510 ų
Envelope volume envelope_volume208860 ų
Hydration-shell volume shell_volume51157 ų
Envelope diameter envelope_diameter112.2
Shell Rg shell_rg40.84
Envelope Rg envelope_rg33.28
Shape Rg shape_rg33.16
Total Rg total_rg33.75
Total atoms total_atoms9093
Residues n_residues1149
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 dmax108.8
Rg (real space) rg_real33.95
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real2.5590e+08
I(0) uncertainty (real space) i0_real_error3.9120e+06
Rg (reciprocal space) rg_reciprocal34.01
I(0) (reciprocal space) i0_reciprocal255900000.0000
Solution quality estimate total_estimate0.8973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.2
Skewness Skewness skewness0.234
Kurtosis Kurtosis kurtosis-0.481
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha63720000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)