← Back to search
7tuj

NMR solution structure of the phosphorylated MUS81-binding region from human SLX4

Method: SOLUTION NMR Dmax: 58.6 Å Quality: REASONABLE
▼

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1528–1613 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.4；283 K；Ionic strength (raw mmCIF value) 0.125；Pressure 1 NMR sample composition：500 uM [U-100% 13C; U-100% 15N] Phosphorylated MUS81-binding region of human SLX4, 25 mM sodium phosphate, 100 mM sodium chloride, 100 uM EDTA, 100 uM sodium azide, 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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.

Other PDB Difference from Current Entry 7TUJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4M7C Crystal structure of the TRF2-binding motif of SLX4 in complex with the TRFH domain of TRF2 Deposited 2013-08-12 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1014–1025（12 aa） Fragment：TRF2-binding motif, UNP residues 1014-1025
Chain D 1014–1025（12 aa） Fragment：TRF2-binding motif, UNP residues 1014-1025
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；277 K；10% PEG 4000, 0.1M HEPES, pH 7.4, 100mM NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.05 Å R-free 0.262
4UYI Crystal structure of the BTB domain of human SLX4 (BTBD12) Deposited 2014-09-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 668–796（129 aa） Fragment：BTB DOMAIN (BTBD12), UNP RESIDUES 668-796
Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.2M MAGNESIUM CHLORIDE, 25% PEG3350, 0.1M BIS-TRIS PH 6.5
Resolution 1.86 Å R-free 0.194
4ZOU Crystal structure of the BTB domain of SLX4 Deposited 2015-05-07 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 669–787（119 aa） Fragment：BTB domain (UNP RESIDUES 669-787)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；277 K；4-6% PEG 6000, 0.1 M HEPES, pH 7.6, 5% glycerol
Resolution 2.15 Å R-free 0.244
7BU5 Crystal Structure of Human SLX4 and MUS81 Deposited 2020-04-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1550–1610（61 aa） Fragment：SAP domain
Not recorded GLY GLYCINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 8.5；277 K；25% w/v PEG 3350, 0.1M SPG (succinic acid: sodium dihydrogen phosphate: glycine, 2: 7: 7)
Resolution 1.80 Å R-free 0.206
9QED Cryo-EM structure of the XPF-ERCC1-SLX4(330-555)-SLX4IP complex Deposited 2025-03-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 330–555（226 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9QEE Cryo-EM structure of a DNA-bound XPF-ERCC1-SLX4(330-555)-SLX4IP complex Deposited 2025-03-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric
Chain D 330–555（226 aa）
Not recorded MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å

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 1
Chains and sequence ranges Author chain A； PDBConstruct 1–86； UniProt 1528–1613

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 7tuj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tuj
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id7tuj
Deposition date deposition_date2022-02-02
Structure title titleNMR solution structure of the phosphorylated MUS81-binding region from human SLX4
Keywords keywordsSAP domain, disorder-to-order transition, protein binding; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
▼

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

Radius of gyration Rg (Guinier) rg_guinier16.10 Å
Radius of gyration Rg (electron density) rg_electron15.71 Å
Forward intensity I(0) i0592971000.00
Molecular weight molecular_weight198950.0 kDa
Excluded volume excluded_volume247380 ų
Envelope volume envelope_volume57705 ų
Hydration-shell volume shell_volume23266 ų
Envelope diameter envelope_diameter63.9 Å
Shell Rg shell_rg27.69 Å
Envelope Rg envelope_rg20.93 Å
Shape Rg shape_rg15.69 Å
Total Rg total_rg16.15 Å
Total atoms total_atoms27880
Residues n_residues1660
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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 dmax58.6 Å
Rg (real space) rg_real16.13 Å
Rg uncertainty (real space) rg_real_error0.55 Å
I(0) (real space) i0_real5.9300e+08
I(0) uncertainty (real space) i0_real_error8.3710e+06
Rg (reciprocal space) rg_reciprocal16.13 Å
I(0) (reciprocal space) i0_reciprocal593000000.0000
Solution quality estimate total_estimate0.7406
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.8 Å
Skewness Skewness skewness0.443
Kurtosis Kurtosis kurtosis-0.039
Angular range angular_range— – 0.4950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha616300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.577; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.000
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▶

8. Citations (1)

▶

9. Files and Curves (10)