8ebx

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

Method: ELECTRON MICROSCOPY Dmax: 191.2 Å Quality: GOOD

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

TFIIH basal transcription factor complex helicase XPB subunit

Homo sapiens

UniProt P19447

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 A; UniProt 1–782 Not recorded 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, p52 × 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) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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 ERCC3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–782; UniProt 1–782

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 1–760 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) General transcription factor IIH subunit 1 × 1 (P32780) General transcription factor IIH subunit 4, p52 × 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) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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 1–760; UniProt 1–760

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 1–548 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) General transcription and DNA repair factor IIH helicase subunit XPD × 1 (P18074) General transcription factor IIH subunit 4, p52 × 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) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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 1–548; UniProt 1–548

General transcription factor IIH subunit 4, p52

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 1–462 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) 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) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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 1–462; UniProt 1–462

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 1–395 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) 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, p52 × 1 (Q92759) General transcription factor IIH subunit 3 × 1 (Q13889) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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 23–417; UniProt 1–395

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 1–308 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) 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, p52 × 1 (Q92759) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 5 × 1 (Q6ZYL4) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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 1–308; UniProt 1–308

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 1–71 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) 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, p52 × 1 (Q92759) General transcription factor IIH subunit 2 × 1 (Q13888) General transcription factor IIH subunit 3 × 1 (Q13889) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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 1–71; UniProt 1–71

Xeroderma pigmentosum, complementation group C, isoform CRA_a

Homo sapiens

UniProt A0A024R2M8

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 H; UniProt 1–940 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) 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, p52 × 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) Centrin-2 × 1 (P41208) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A024R2M8_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 11–950; UniProt 1–940

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 1–172 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) 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, p52 × 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) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) DNA repair protein complementing XP-A cells × 1 (P23025) DNA (Ap) × 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 3.60 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 1–172; UniProt 1–172

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 1–273 Not recorded TFIIH basal transcription factor complex helicase XPB subunit × 1 (P19447) 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, p52 × 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) Xeroderma pigmentosum, complementation group C, isoform CRA_a × 1 (A0A024R2M8) Centrin-2 × 1 (P41208) DNA (Ap) × 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 3.60 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 1–273; UniProt 1–273

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 8ebx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ebx
Deposition date deposition_date2022-08-31
Structure title titleXPA repositioning Core7 of TFIIH relative to XPC-DNA lesion (AP)
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_guinier56.39
Radius of gyration Rg (electron density) rg_electron56.24
Forward intensity I(0) i02337360000.00
Molecular weight molecular_weight393600.0 kDa
Excluded volume excluded_volume487830 ų
Envelope volume envelope_volume777570 ų
Hydration-shell volume shell_volume113170 ų
Envelope diameter envelope_diameter195.0
Shell Rg shell_rg59.88
Envelope Rg envelope_rg55.61
Shape Rg shape_rg56.24
Total Rg total_rg56.34
Total atoms total_atoms27524
Residues n_residues3297
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 dmax191.2
Rg (real space) rg_real56.30
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real2.3370e+09
I(0) uncertainty (real space) i0_real_error4.3380e+07
Rg (reciprocal space) rg_reciprocal56.44
I(0) (reciprocal space) i0_reciprocal2338000000.0000
Solution quality estimate total_estimate0.8798
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.3
Skewness Skewness skewness0.271
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha204600000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.854

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)