9qed

Cryo-EM structure of the XPF-ERCC1-SLX4(330-555)-SLX4IP complex

Method: ELECTRON MICROSCOPY Dmax: 110.4 Å Quality: GOOD

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

Protein SLX4IP

Homo sapiens

UniProt Q5VYV7

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–408 Not recorded DNA repair endonuclease XPF × 1 (Q92889) DNA excision repair protein ERCC-1 × 1 (P07992) Structure-specific endonuclease subunit SLX4 × 1 (Q8IY92) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SLX4I_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–408; UniProt 1–408

DNA repair endonuclease XPF

Homo sapiens

UniProt Q92889

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–916 Not recorded Protein SLX4IP × 1 (Q5VYV7) DNA excision repair protein ERCC-1 × 1 (P07992) Structure-specific endonuclease subunit SLX4 × 1 (Q8IY92) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

12 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XPF_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 20–935; UniProt 1–916

DNA excision repair protein ERCC-1

Homo sapiens

UniProt P07992

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–297 Not recorded Protein SLX4IP × 1 (Q5VYV7) DNA repair endonuclease XPF × 1 (Q92889) Structure-specific endonuclease subunit SLX4 × 1 (Q8IY92) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERCC1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–297; UniProt 1–297

Structure-specific endonuclease subunit SLX4

Homo sapiens

UniProt Q8IY92

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 330–555 Not recorded Protein SLX4IP × 1 (Q5VYV7) DNA repair endonuclease XPF × 1 (Q92889) DNA excision repair protein ERCC-1 × 1 (P07992) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SLX4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 46–271; UniProt 330–555

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 9qed

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qed
Deposition date deposition_date2025-03-09
Structure title titleCryo-EM structure of the XPF-ERCC1-SLX4(330-555)-SLX4IP complex
Keywords keywordsDNA repair, endonuclease, multiprotein complex, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.07
Radius of gyration Rg (electron density) rg_electron33.38
Forward intensity I(0) i0226706000.00
Molecular weight molecular_weight124180.0 kDa
Excluded volume excluded_volume157220 ų
Envelope volume envelope_volume207980 ų
Hydration-shell volume shell_volume51472 ų
Envelope diameter envelope_diameter117.5
Shell Rg shell_rg40.63
Envelope Rg envelope_rg32.76
Shape Rg shape_rg33.39
Total Rg total_rg33.94
Total atoms total_atoms8748
Residues n_residues1088
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 dmax110.4
Rg (real space) rg_real33.97
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real2.2670e+08
I(0) uncertainty (real space) i0_real_error3.6390e+06
Rg (reciprocal space) rg_reciprocal34.03
I(0) (reciprocal space) i0_reciprocal226700000.0000
Solution quality estimate total_estimate0.8809
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.6
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-0.230
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha94530000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)