2rnr

Solution structure of the complex between TFIIE alpha C-terminal acidic domain and TFIIH p62 PH domain

Method: SOLUTION NMR Dmax: 55.5 Å Quality: EXCELLENT

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

Transcription initiation factor IIE subunit alpha

Homo sapiens

UniProt P29083

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 378–439 Fragment:C-terminal acidic domain, UNP residues 378-439 TFIIH basal transcription factor complex p62 subunit × 1 (P32780) SOLUTION NMR NMR measurement conditions:pH 6.8;305 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR sample composition:0.5MM [U-100% 15N] TFIIE-ALPHA, 0.5MM TFIIH P62; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5MM [U-100% 13C; U-100% 15N] TFIIE-ALPHA, 0.5MM TFIIH P62; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5MM [U-100% 13C; U-100% 15N] TFIIE-ALPHA, 0.5MM TFIIH P62; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 100% D2O | 100% D2O NMR sample composition:0.5MM [U-100% 15N] TFIIH P62, 0.5mM TFIIE-ALPHA; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5MM [U-100% 13C; U-100% 15N] TFIIH P62, 0.5MM TFIIE-ALPHA; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5MM [U-100% 13C; U-100% 15N] TFIIH P62, 0.5MM TFIIE-ALPHA; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 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.

47 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name T2EA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–64; UniProt 378–439

TFIIH basal transcription factor complex p62 subunit

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–108 Fragment:PH domain, UNP residues 1-108 Transcription initiation factor IIE subunit alpha × 1 (P29083) SOLUTION NMR NMR measurement conditions:pH 6.8;305 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR sample composition:0.5MM [U-100% 15N] TFIIE-ALPHA, 0.5MM TFIIH P62; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5MM [U-100% 13C; U-100% 15N] TFIIE-ALPHA, 0.5MM TFIIH P62; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5MM [U-100% 13C; U-100% 15N] TFIIE-ALPHA, 0.5MM TFIIH P62; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 100% D2O | 100% D2O NMR sample composition:0.5MM [U-100% 15N] TFIIH P62, 0.5mM TFIIE-ALPHA; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5MM [U-100% 13C; U-100% 15N] TFIIH P62, 0.5MM TFIIE-ALPHA; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5MM [U-100% 13C; U-100% 15N] TFIIH P62, 0.5MM TFIIE-ALPHA; 20MM POTASSIUM PHOSPHATE, 5MM [U-99% 2H] DTT, 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 3–110; UniProt 1–108

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 2rnr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2rnr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2rnr
Deposition date deposition_date2008-01-31
Structure title titleSolution structure of the complex between TFIIE alpha C-terminal acidic domain and TFIIH p62 PH domain
Keywords keywordsgeneral transcription factor, human TFIIE alpha, human TFIIH p62, acidic domain, PH domain, DNA DAMAGE, DNA REPAIR, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.22
Radius of gyration Rg (electron density) rg_electron16.96
Forward intensity I(0) i02146290000.00
Molecular weight molecular_weight390160.0 kDa
Excluded volume excluded_volume486490 ų
Envelope volume envelope_volume44368 ų
Hydration-shell volume shell_volume19327 ų
Envelope diameter envelope_diameter62.7
Shell Rg shell_rg25.65
Envelope Rg envelope_rg19.55
Shape Rg shape_rg16.94
Total Rg total_rg17.13
Total atoms total_atoms54340
Residues n_residues3400
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 dmax55.5
Rg (real space) rg_real17.22
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.1460e+09
I(0) uncertainty (real space) i0_real_error2.6090e+07
Rg (reciprocal space) rg_reciprocal17.22
I(0) (reciprocal space) i0_reciprocal2146000000.0000
Solution quality estimate total_estimate0.9057
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.7
Skewness Skewness skewness0.294
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha587400.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2rnrb_
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.9 — TFIIH domain

CATH v4.4 (1 domains)

Domain ID domain_id2rnrB00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

8. Citations (1)

9. Files and Curves (10)