8d7x

Cereblon~DDB1 in the Apo form with DDB1 in the hinged conformation

Method: ELECTRON MICROSCOPY Dmax: 135.9 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–1140 Not recorded Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;20mM HEPES pH 7, 240mM NaCl, 3mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE;Manual plunge in 4 degree C cold room Resolution 3.40 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.

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 1–1140; UniProt 1–1140

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–442 Not recorded DNA damage-binding protein 1 × 1 (Q16531) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;20mM HEPES pH 7, 240mM NaCl, 3mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE;Manual plunge in 4 degree C cold room Resolution 3.40 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.

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 1–442; UniProt 1–442

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 8d7x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8d7x
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8d7x
Deposition date deposition_date2022-06-07
Structure title titleCereblon~DDB1 in the Apo form with DDB1 in the hinged conformation
Keywords keywordsUbiquitin, CRL4, Adaptor, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.26
Radius of gyration Rg (electron density) rg_electron37.00
Forward intensity I(0) i0344930000.00
Molecular weight molecular_weight143210.0 kDa
Excluded volume excluded_volume176000 ų
Envelope volume envelope_volume254490 ų
Hydration-shell volume shell_volume57209 ų
Envelope diameter envelope_diameter144.1
Shell Rg shell_rg42.55
Envelope Rg envelope_rg38.10
Shape Rg shape_rg37.14
Total Rg total_rg36.91
Total atoms total_atoms10108
Residues n_residues1484
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 dmax135.9
Rg (real space) rg_real38.36
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real3.4490e+08
I(0) uncertainty (real space) i0_real_error6.4000e+06
Rg (reciprocal space) rg_reciprocal38.30
I(0) (reciprocal space) i0_reciprocal344900000.0000
Solution quality estimate total_estimate0.8445
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.4
Skewness Skewness skewness0.507
Kurtosis Kurtosis kurtosis0.119
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70800000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.710; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8d7xA01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8d7xA02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8d7xA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily910

8. Citations (2)

9. Files and Curves (10)