2lox

NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and Rad2

Method: SOLUTION NMR Dmax: 55.7 Å Quality: GOOD

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

RNA polymerase II transcription factor B subunit 1

Saccharomyces cerevisiae

UniProt P32776

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 2–115 Fragment:UNP residues 2-115 DNA repair protein RAD2 × 1 (P07276) SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Pressure ambient NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 100% D2O | 100% D2O NMR sample composition:1 mM [U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1.25 mM Tfb1, 1 mM [U-100% 13C; U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1.25 mM Tfb1, 1 mM [U-100% 13C; U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 100% D2O | 100% D2O NMR sample composition:1.25 mM Tfb1, 1 mM [U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% 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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TFB1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–115; UniProt 2–115

DNA repair protein RAD2

Saccharomyces cerevisiae

UniProt P07276

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 642–690 Fragment:UNP residues 642-690 RNA polymerase II transcription factor B subunit 1 × 1 (P32776) SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Pressure ambient NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 100% D2O | 100% D2O NMR sample composition:1 mM [U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1.25 mM Tfb1, 1 mM [U-100% 13C; U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1.25 mM Tfb1, 1 mM [U-100% 13C; U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 100% D2O | 100% D2O NMR sample composition:1.25 mM Tfb1, 1 mM [U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% 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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAD2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–51; UniProt 642–690

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 2lox

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lox
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2lox
Deposition date deposition_date2012-01-27
Structure title titleNMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and Rad2
Keywords keywordsTRANSCRIPTION-HYDROLASE complex; TRANSCRIPTION/HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.82
Radius of gyration Rg (electron density) rg_electron16.13
Forward intensity I(0) i01320840000.00
Molecular weight molecular_weight302480.0 kDa
Excluded volume excluded_volume376950 ų
Envelope volume envelope_volume45478 ų
Hydration-shell volume shell_volume19358 ų
Envelope diameter envelope_diameter64.6
Shell Rg shell_rg26.51
Envelope Rg envelope_rg20.94
Shape Rg shape_rg16.12
Total Rg total_rg16.34
Total atoms total_atoms42640
Residues n_residues2700
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 dmax55.7
Rg (real space) rg_real16.86
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.3210e+09
I(0) uncertainty (real space) i0_real_error1.5170e+07
Rg (reciprocal space) rg_reciprocal16.86
I(0) (reciprocal space) i0_reciprocal1321000000.0000
Solution quality estimate total_estimate0.8021
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.5
Skewness Skewness skewness0.419
Kurtosis Kurtosis kurtosis-0.238
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha520800.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.821; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2loxa1
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
Domain ID domain_idd2loxa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2loxA00
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)