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6tur

human XPG, Apo1 form

Method: X-RAY DIFFRACTION Dmax: 118.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

DNA repair protein complementing XP-G cells,DNA repair protein complementing XP-G cells

Homo sapiens

UniProt P28715

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 AAA； UniProt 2–112 Chain AAA； UniProt 750–990 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；25% PEG 3350, 100 mM Citric acid pH 3.5 Resolution 2.90 Å R-free 0.281
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain BBB； UniProt 2–112 Chain BBB； UniProt 750–990 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；25% PEG 3350, 100 mM Citric acid pH 3.5 Resolution 2.90 Å R-free 0.281
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain CCC； UniProt 2–112 Chain CCC； UniProt 750–990 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；25% PEG 3350, 100 mM Citric acid pH 3.5 Resolution 2.90 Å R-free 0.281
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain DDD； UniProt 2–112 Chain DDD； UniProt 750–990 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；25% PEG 3350, 100 mM Citric acid pH 3.5 Resolution 2.90 Å R-free 0.281

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 6TUR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5EKF Crystallization and X-ray Diffraction Data Collection of Importin-alpha from Mus musculus Complexed with a XPG NLS Peptide, fragment 1 Deposited 2015-11-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1054–1077（24 aa） Fragment：UNP residues 1054-1077
Chain C 1054–1077（24 aa） Fragment：UNP residues 1054-1077
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.6-0.7 M sodium citrate, 10 mM DTT
Resolution 2.00 Å R-free 0.192
6TUS human XPG, Apo2 form Deposited 2020-01-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–112（112 aa）
Chain A 750–990（241 aa）
Not recorded SO4 SULFATE ION × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；25% PEG 3350, 100 mM Bis-Tris pH 6.5, 200 mM Amm. Sulfate.
Resolution 2.50 Å R-free 0.237
6TUS human XPG, Apo2 form Deposited 2020-01-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–112（112 aa）
Chain B 750–990（241 aa）
Not recorded SO4 SULFATE ION × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；25% PEG 3350, 100 mM Bis-Tris pH 6.5, 200 mM Amm. Sulfate.
Resolution 2.50 Å R-free 0.237
6TUW human XPG-DNA, Complex 1 Deposited 2020-01-08 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric
Chain A 1–112（112 aa）
Chain A 750–990（241 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；5% PEG 3350, 50 mM Na Citrate pH 4.0
Resolution 3.50 Å R-free 0.293
6TUX human XPG-DNA, Complex 2 Deposited 2020-01-08 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric
Chain A 1–112（112 aa）
Chain A 750–986（237 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；5% PEG 3350, 50 mM Na Citrate pH 4.0
Resolution 3.10 Å R-free 0.303
6TUX human XPG-DNA, Complex 2 Deposited 2020-01-08 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric
Chain B 1–112（112 aa）
Chain B 750–986（237 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；5% PEG 3350, 50 mM Na Citrate pH 4.0
Resolution 3.10 Å R-free 0.303
6VBH Human XPG endonuclease catalytic domain Deposited 2019-12-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–85（84 aa）
Chain A 766–987（222 aa）
Not recorded SO4 SULFATE ION × 15 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；288 K；Mixed 1:1 with 40% AmSO4, 200 mM Imidizole/Malate Buffer pH 4.2,100 mM MgCl2
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；288 K；Mixed 1:1 wit 24% AmSO4, 200 mM Imidizole/Malate Buffer pH 4.2, 250 mM MgCl2, 0.5 mM SmSO4, 10 mM DTT
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；288 K；Mixed 1:1 with 32% AmSO4, 10 mM DTT, 200 mM Imidizole/Malate Buffer pH 4.2, and 50 mM MgCl2
Resolution 2.00 Å R-free 0.244
6VBH Human XPG endonuclease catalytic domain Deposited 2019-12-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–85（84 aa）
Chain A 766–987（222 aa）
Not recorded SO4 SULFATE ION × 30 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；288 K；Mixed 1:1 with 40% AmSO4, 200 mM Imidizole/Malate Buffer pH 4.2,100 mM MgCl2
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；288 K；Mixed 1:1 wit 24% AmSO4, 200 mM Imidizole/Malate Buffer pH 4.2, 250 mM MgCl2, 0.5 mM SmSO4, 10 mM DTT
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；288 K；Mixed 1:1 with 32% AmSO4, 10 mM DTT, 200 mM Imidizole/Malate Buffer pH 4.2, and 50 mM MgCl2
Resolution 2.00 Å R-free 0.244
9PD3 NER dual incision complex - DuIS Deposited 2025-06-30 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 × 15 PDB declaration: 17-meric
Chain S 1–1186（1186 aa）
Mutation：D812N SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9PD4 NER dual incision complex - DuIM Deposited 2025-06-30 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 × 14 PDB declaration: hexadecameric
Chain S 1–1186（1186 aa）
Mutation：D812N SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9PD5 NER dual incision complex - NoF Deposited 2025-06-30 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 × 9 PDB declaration: 11-meric
Chain S 1–1186（1186 aa）
Not recorded SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.70 Å

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERCC5_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain AAA； PDBConstruct 2–112； UniProt 2–112 Author chain AAA； PDBConstruct 115–355； UniProt 750–990 Author chain BBB； PDBConstruct 2–112； UniProt 2–112 Author chain BBB； PDBConstruct 115–355； UniProt 750–990 Author chain CCC； PDBConstruct 2–112； UniProt 2–112 Author chain CCC； PDBConstruct 115–355； UniProt 750–990 Author chain DDD； PDBConstruct 2–112； UniProt 2–112 Author chain DDD； PDBConstruct 115–355； UniProt 750–990

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 6tur

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6tur
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6tur
Deposition date deposition_date2020-01-08
Structure title titlehuman XPG, Apo1 form
Keywords keywordsXPG nuclease domain, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier37.07 Å
Radius of gyration Rg (electron density) rg_electron36.28 Å
Forward intensity I(0) i0305222000.00
Molecular weight molecular_weight146100.0 kDa
Excluded volume excluded_volume184850 ų
Envelope volume envelope_volume259510 ų
Hydration-shell volume shell_volume57953 ų
Envelope diameter envelope_diameter132.3 Å
Shell Rg shell_rg43.48 Å
Envelope Rg envelope_rg36.31 Å
Shape Rg shape_rg36.27 Å
Total Rg total_rg36.84 Å
Total atoms total_atoms10271
Residues n_residues1251
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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax118.5 Å
Rg (real space) rg_real36.92 Å
Rg uncertainty (real space) rg_real_error0.85 Å
I(0) (real space) i0_real3.0520e+08
I(0) uncertainty (real space) i0_real_error5.0150e+06
Rg (reciprocal space) rg_reciprocal37.02 Å
I(0) (reciprocal space) i0_reciprocal305200000.0000
Solution quality estimate total_estimate0.8872
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.6 Å
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.297
Angular range angular_range— – 0.2150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha68070000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.889
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)