8ebt

XPA repositioning Core7 of TFIIH relative to XPC-DNA lesion (Cy5)

Method: ELECTRON MICROSCOPY Dmax: 190.7 Å Quality: REASONABLE

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

General transcription and DNA repair factor IIH helicase subunit XPD

Homo sapiens

UniProt P18074

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 1–730 Not recorded General transcription and DNA repair factor IIH helicase subunit XPB × 1 General transcription factor IIH subunit 1 × 1 (P32780) General transcription factor IIH subunit 4 × 1 (Q92759) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 3 × 1 (Q13889) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) DNA repair protein complementing XP-C cells × 1 Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Cy5) × 1 DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

49 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERCC2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–730; UniProt 1–730

General transcription factor IIH subunit 1

Homo sapiens

UniProt P32780

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 111–548 Not recorded General transcription and DNA repair factor IIH helicase subunit XPB × 1 General transcription and DNA repair factor IIH helicase subunit XPD × 1 (P18074) General transcription factor IIH subunit 4 × 1 (Q92759) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 3 × 1 (Q13889) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) DNA repair protein complementing XP-C cells × 1 Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Cy5) × 1 DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF2H1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–438; UniProt 111–548

General transcription factor IIH subunit 4

Homo sapiens

UniProt Q92759

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 17–462 Not recorded General transcription and DNA repair factor IIH helicase subunit XPB × 1 General transcription and DNA repair factor IIH helicase subunit XPD × 1 (P18074) General transcription factor IIH subunit 1 × 1 (P32780) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 3 × 1 (Q13889) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) DNA repair protein complementing XP-C cells × 1 Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Cy5) × 1 DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

50 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF2H4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–446; UniProt 17–462

General transcription factor IIH subunit 2

Homo sapiens

UniProt Q13888

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain E; UniProt 8–387 Not recorded General transcription and DNA repair factor IIH helicase subunit XPB × 1 General transcription and DNA repair factor IIH helicase subunit XPD × 1 (P18074) General transcription factor IIH subunit 1 × 1 (P32780) General transcription factor IIH subunit 4 × 1 (Q92759) General transcription factor IIH subunit 3 × 1 (Q13889) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) DNA repair protein complementing XP-C cells × 1 Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Cy5) × 1 DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

50 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF2H2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–380; UniProt 8–387

General transcription factor IIH subunit 3

Homo sapiens

UniProt Q13889

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain F; UniProt 6–289 Not recorded General transcription and DNA repair factor IIH helicase subunit XPB × 1 General transcription and DNA repair factor IIH helicase subunit XPD × 1 (P18074) General transcription factor IIH subunit 1 × 1 (P32780) General transcription factor IIH subunit 4 × 1 (Q92759) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) DNA repair protein complementing XP-C cells × 1 Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Cy5) × 1 DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

50 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF2H3_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–284; UniProt 6–289

General transcription factor IIH subunit 5

Homo sapiens

UniProt Q6ZYL4

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain G; UniProt 4–69 Not recorded General transcription and DNA repair factor IIH helicase subunit XPB × 1 General transcription and DNA repair factor IIH helicase subunit XPD × 1 (P18074) General transcription factor IIH subunit 1 × 1 (P32780) General transcription factor IIH subunit 4 × 1 (Q92759) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 3 × 1 (Q13889) DNA repair protein complementing XP-C cells × 1 Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Cy5) × 1 DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

52 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF2H5_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–66; UniProt 4–69

Centrin-2

Homo sapiens

UniProt P41208

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain J; UniProt 103–172 Not recorded General transcription and DNA repair factor IIH helicase subunit XPB × 1 General transcription and DNA repair factor IIH helicase subunit XPD × 1 (P18074) General transcription factor IIH subunit 1 × 1 (P32780) General transcription factor IIH subunit 4 × 1 (Q92759) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 3 × 1 (Q13889) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) DNA repair protein complementing XP-C cells × 1 DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Cy5) × 1 DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CETN2_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain J; PDBConstruct 1–70; UniProt 103–172

DNA repair protein complementing XP-A cells

Homo sapiens

UniProt P23025

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 102–273 Not recorded General transcription and DNA repair factor IIH helicase subunit XPB × 1 General transcription and DNA repair factor IIH helicase subunit XPD × 1 (P18074) General transcription factor IIH subunit 1 × 1 (P32780) General transcription factor IIH subunit 4 × 1 (Q92759) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 3 × 1 (Q13889) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) DNA repair protein complementing XP-C cells × 1 Centrin-2 × 1 (P41208) DNA (Cy5) × 1 DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 6 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XPA_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain K; PDBConstruct 1–172; UniProt 102–273

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 8ebt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ebt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ebt
Deposition date deposition_date2022-08-31
Structure title titleXPA repositioning Core7 of TFIIH relative to XPC-DNA lesion (Cy5)
Keywords keywordsprotein-DNA complex, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.35
Radius of gyration Rg (electron density) rg_electron55.87
Forward intensity I(0) i02276530000.00
Molecular weight molecular_weight386450.0 kDa
Excluded volume excluded_volume478100 ų
Envelope volume envelope_volume754540 ų
Hydration-shell volume shell_volume110900 ų
Envelope diameter envelope_diameter195.4
Shell Rg shell_rg59.49
Envelope Rg envelope_rg55.11
Shape Rg shape_rg55.85
Total Rg total_rg56.02
Total atoms total_atoms27017
Residues n_residues3215
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 dmax190.7
Rg (real space) rg_real58.34
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real2.2690e+09
I(0) uncertainty (real space) i0_real_error3.9370e+07
Rg (reciprocal space) rg_reciprocal56.36
I(0) (reciprocal space) i0_reciprocal2277000000.0000
Solution quality estimate total_estimate0.6843
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.1
Skewness Skewness skewness0.431
Kurtosis Kurtosis kurtosis-0.189
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha1.2810
Highest regularization parameter α highest_alpha192800000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 0.890; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.549

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id8ebtA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id8ebtA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id8ebtE01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily410 — von Willebrand factor, type A domain
Domain ID domain_id8ebtE02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id8ebtK01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology530 — Nucleotide Excision Repair Protein XPA (XPA-MBD); B Chain A
Homologous superfamily homologous superfamily10 — XPA C-terminal domain

8. Citations (1)

9. Files and Curves (10)