7dti

Solution structure of the complex between RNA polymerase subunit RPB6 and TFIIH p62 PH domain

Method: SOLUTION NMR Dmax: 97.1 Å Quality: GOOD

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

DNA-directed RNA polymerases I, II, and III subunit RPABC2

Homo sapiens

UniProt P61218

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–127 Not recorded General transcription factor IIH subunit 1 × 1 (A0A2K6V299) SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 25;Pressure 1 NMR sample composition:0.38 mM [U-100% 13C; U-100% 15N] RPB6, 0.38 mM TFIIH p62, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.38 mM [U-100% 13C; U-100% 15N] RPB6, 0.38 mM TFIIH p62, 100% D2O | 100% D2O NMR sample composition:0.38 mM [U-100% 13C; U-100% 15N] TFIIH p62, 0.38 mM RPB6, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.38 mM [U-100% 13C; U-100% 15N] TFIIH p62, 0.38 mM RPB6, 100% D2O | 100% 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.

58 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPAB2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–130; UniProt 1–127

General transcription factor IIH subunit 1

Homo sapiens

UniProt A0A2K6V299

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 8–115 Not recorded DNA-directed RNA polymerases I, II, and III subunit RPABC2 × 1 (P61218) SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 25;Pressure 1 NMR sample composition:0.38 mM [U-100% 13C; U-100% 15N] RPB6, 0.38 mM TFIIH p62, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.38 mM [U-100% 13C; U-100% 15N] RPB6, 0.38 mM TFIIH p62, 100% D2O | 100% D2O NMR sample composition:0.38 mM [U-100% 13C; U-100% 15N] TFIIH p62, 0.38 mM RPB6, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.38 mM [U-100% 13C; U-100% 15N] TFIIH p62, 0.38 mM RPB6, 100% D2O | 100% 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A2K6V299_SAIBB
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–111; UniProt 8–115

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 7dti

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7dti
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7dti
Deposition date deposition_date2021-01-05
Structure title titleSolution structure of the complex between RNA polymerase subunit RPB6 and TFIIH p62 PH domain
Keywords keywordsRNA polymerase, general transcription factor, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier29.24
Radius of gyration Rg (electron density) rg_electron29.14
Forward intensity I(0) i04139070000.00
Molecular weight molecular_weight534970.0 kDa
Excluded volume excluded_volume666490 ų
Envelope volume envelope_volume270460 ų
Hydration-shell volume shell_volume59310 ų
Envelope diameter envelope_diameter110.6
Shell Rg shell_rg44.36
Envelope Rg envelope_rg37.13
Shape Rg shape_rg29.06
Total Rg total_rg29.73
Total atoms total_atoms74840
Residues n_residues4700
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 dmax97.1
Rg (real space) rg_real29.34
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real4.1390e+09
I(0) uncertainty (real space) i0_real_error6.8780e+07
Rg (reciprocal space) rg_reciprocal29.30
I(0) (reciprocal space) i0_reciprocal4139000000.0000
Solution quality estimate total_estimate0.8122
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.696
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3251000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.791; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.761; Smooth: 0.422

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)