9xzj

Cryo-EM structure of F-box helicase 1 (FBH1) bound to an SCF ubiquitin ligase complex and a 3-way DNA fork (consensus structure)

Method: ELECTRON MICROSCOPY Dmax: 209.7 Å Quality: GOOD

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

Cullin-1

Homo sapiens

UniProt Q13616

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–DNA Heteromer Protein × 4 DNA 4 PDB declaration: octameric(8) Consistent with all polymer counts Chain C; UniProt 1–776 Not recorded E3 ubiquitin-protein ligase RBX1 × 1 (P62877) F-box DNA helicase 1 × 1 (Q8NFZ0) S-phase kinase-associated protein 1 × 1 (P63208) DNA (45-MER) × 1 ;DNA (5'-D(*CP*TP*GP*AP*CP*GP*CP*TP*TP*CP*CP*AP*TP*CP*GP*CP*TP*GP*TP*CP*TP*AP*G)-3') ; × 1 ;DNA (5'-D(*TP*CP*GP*CP*TP*AP*CP*CP*TP*TP*CP*GP*CP*AP*GP*TP*C)-3') ; × 1 DNA (45-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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.

47 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–776; UniProt 1–776

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–DNA Heteromer Protein × 4 DNA 4 PDB declaration: octameric(8) Consistent with all polymer counts Chain R; UniProt 1–108 Not recorded Cullin-1 × 1 (Q13616) F-box DNA helicase 1 × 1 (Q8NFZ0) S-phase kinase-associated protein 1 × 1 (P63208) DNA (45-MER) × 1 ;DNA (5'-D(*CP*TP*GP*AP*CP*GP*CP*TP*TP*CP*CP*AP*TP*CP*GP*CP*TP*GP*TP*CP*TP*AP*G)-3') ; × 1 ;DNA (5'-D(*TP*CP*GP*CP*TP*AP*CP*CP*TP*TP*CP*GP*CP*AP*GP*TP*C)-3') ; × 1 DNA (45-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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 2
Chains and sequence ranges Author chain R; PDBConstruct 1–108; UniProt 1–108

F-box DNA helicase 1

Homo sapiens

UniProt Q8NFZ0

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–DNA Heteromer Protein × 4 DNA 4 PDB declaration: octameric(8) Consistent with all polymer counts Chain F; UniProt 75–1043 Not recorded Cullin-1 × 1 (Q13616) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) S-phase kinase-associated protein 1 × 1 (P63208) DNA (45-MER) × 1 ;DNA (5'-D(*CP*TP*GP*AP*CP*GP*CP*TP*TP*CP*CP*AP*TP*CP*GP*CP*TP*GP*TP*CP*TP*AP*G)-3') ; × 1 ;DNA (5'-D(*TP*CP*GP*CP*TP*AP*CP*CP*TP*TP*CP*GP*CP*AP*GP*TP*C)-3') ; × 1 DNA (45-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FBH1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 4–972; UniProt 75–1043

S-phase kinase-associated protein 1

Homo sapiens

UniProt P63208

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–DNA Heteromer Protein × 4 DNA 4 PDB declaration: octameric(8) Consistent with all polymer counts Chain S; UniProt 1–163 Not recorded Cullin-1 × 1 (Q13616) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) F-box DNA helicase 1 × 1 (Q8NFZ0) DNA (45-MER) × 1 ;DNA (5'-D(*CP*TP*GP*AP*CP*GP*CP*TP*TP*CP*CP*AP*TP*CP*GP*CP*TP*GP*TP*CP*TP*AP*G)-3') ; × 1 ;DNA (5'-D(*TP*CP*GP*CP*TP*AP*CP*CP*TP*TP*CP*GP*CP*AP*GP*TP*C)-3') ; × 1 DNA (45-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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.

71 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain S; PDBConstruct 1–163; UniProt 1–163

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 9xzj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9xzj
Deposition date deposition_date2025-08-27
Structure title titleCryo-EM structure of F-box helicase 1 (FBH1) bound to an SCF ubiquitin ligase complex and a 3-way DNA fork (consensus structure)
Keywords keywordsHelicase, Translocase, Fork remodeler, Fork reversal, Replication fork, DNA binding, ISOMERASE-DNA complex; ISOMERASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.47
Radius of gyration Rg (electron density) rg_electron62.33
Forward intensity I(0) i0981194000.00
Molecular weight molecular_weight237310.0 kDa
Excluded volume excluded_volume286960 ų
Envelope volume envelope_volume498430 ų
Hydration-shell volume shell_volume73137 ų
Envelope diameter envelope_diameter245.7
Shell Rg shell_rg54.90
Envelope Rg envelope_rg62.62
Shape Rg shape_rg62.22
Total Rg total_rg62.48
Total atoms total_atoms31942
Residues n_residues1849
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 dmax209.7
Rg (real space) rg_real63.96
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real9.7990e+08
I(0) uncertainty (real space) i0_real_error1.9850e+07
Rg (reciprocal space) rg_reciprocal62.79
I(0) (reciprocal space) i0_reciprocal978700000.0000
Solution quality estimate total_estimate0.8374
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary83.9
Skewness Skewness skewness0.478
Kurtosis Kurtosis kurtosis-0.239
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0061
Highest regularization parameter α highest_alpha36450000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.310

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)