9zle

Crystal structure of DCAF1 in complex with SDIPTAC C8

Method: X-RAY DIFFRACTION Dmax: 152.5 Å Quality: GOOD

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

DDB1- and CUL4-associated factor 1

Homo sapiens

UniProt Q9Y4B6

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1077–1390 Chain B; UniProt 1077–1390 Chain C; UniProt 1077–1390 Chain D; UniProt 1077–1390 Chain E; UniProt 1077–1390 Chain F; UniProt 1077–1390 Mutation:F1077A, R1079A A1C24 (4P)-N-[(1S)-3-amino-1-(3-chloro-4-fluorophenyl)-3-oxopropyl]-4-(4-chloro-2-fluorophenyl)-1H-pyrrole-3-carboxamide × 4 A1C25 (4P,4'P)-5,5'-[(1E,33E)-3,32-dioxo-7,10,13,16,19,22,25,28-octaoxa-4,31-diazatetratriaconta-1,33-diene-1,34-diyl]bis{N-[(1S)-3-amino-1-(3-chloro-4-fluorophenyl)-3-oxopropyl]-4-(4-chloro-2-fluorophenyl)-1H-pyrrole-3-carboxamide} × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;294.15 K;1.0 M ammonium tartrate dibasic, 0.1 M sodium acetate trihydrate, pH 4.6 Resolution 2.55 Å R-free 0.305

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.

46 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCAF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–314; UniProt 1077–1390 Author chain B; PDBConstruct 1–314; UniProt 1077–1390 Author chain C; PDBConstruct 1–314; UniProt 1077–1390 Author chain D; PDBConstruct 1–314; UniProt 1077–1390 Author chain E; PDBConstruct 1–314; UniProt 1077–1390 Author chain F; PDBConstruct 1–314; UniProt 1077–1390

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 9zle

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zle
Deposition date deposition_date2025-12-08
Structure title titleCrystal structure of DCAF1 in complex with SDIPTAC C8
Keywords keywordsSDIPTAC, PROTAC, HIV, E3 ligase, inhibitor, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.31
Radius of gyration Rg (electron density) rg_electron45.13
Forward intensity I(0) i01197460000.00
Molecular weight molecular_weight189680.0 kDa
Excluded volume excluded_volume183310 ų
Envelope volume envelope_volume341240 ų
Hydration-shell volume shell_volume63334 ų
Envelope diameter envelope_diameter160.2
Shell Rg shell_rg49.18
Envelope Rg envelope_rg44.24
Shape Rg shape_rg45.06
Total Rg total_rg45.39
Total atoms total_atoms14423
Residues n_residues1775
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 dmax152.5
Rg (real space) rg_real45.39
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real1.1970e+09
I(0) uncertainty (real space) i0_real_error2.1040e+07
Rg (reciprocal space) rg_reciprocal45.31
I(0) (reciprocal space) i0_reciprocal1197000000.0000
Solution quality estimate total_estimate0.8690
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.9
Skewness Skewness skewness0.328
Kurtosis Kurtosis kurtosis-0.431
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48470000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.707

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)