2mkr

Structural Characterization of a Complex Between the Acidic Transactivation Domain of EBNA2 and the Tfb1/p62 subunit of TFIIH.

Method: SOLUTION NMR Dmax: 57.0 Å Quality: GOOD

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

RNA polymerase II transcription factor B subunit 1

Saccharomyces cerevisiae S288c

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 1–115 Not recorded Epstein-Barr nuclear antigen 2 × 1 (P12978) SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Ionic strength (raw mmCIF value) 20;Pressure ambient NMR sample composition:0.7 mM [U-13C; U-15N] Tfb1, 2.1 mM EBNA2, 20 mM sodium phosphate, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM [U-15N] Tfb1, 2.1 mM EBNA2, 20 mM sodium phosphate, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM [U-13C; U-15N] Tfb1, 2.1 mM EBNA2, 20 mM sodium phosphate, 1 mM DTT, 100% D2O | 100% D2O NMR sample composition:0.5 mM [U-13C; U-15N] EBNA2, 1.5 mM Tfb1, 20 mM sodium phosphate, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5 mM [U-100% 15N] EBNA2, 1.5 mM Tfb1, 20 mM sodium phosphate, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5 mM [U-13C; U-15N] EBNA2, 1.5 mM Tfb1, 20 mM sodium phosphate, 1 mM DTT-24, 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.

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 1–115; UniProt 1–115

Epstein-Barr nuclear antigen 2

Human herpesvirus 4

UniProt P12978

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 453–465 Not recorded RNA polymerase II transcription factor B subunit 1 × 1 (P32776) SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Ionic strength (raw mmCIF value) 20;Pressure ambient NMR sample composition:0.7 mM [U-13C; U-15N] Tfb1, 2.1 mM EBNA2, 20 mM sodium phosphate, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM [U-15N] Tfb1, 2.1 mM EBNA2, 20 mM sodium phosphate, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM [U-13C; U-15N] Tfb1, 2.1 mM EBNA2, 20 mM sodium phosphate, 1 mM DTT, 100% D2O | 100% D2O NMR sample composition:0.5 mM [U-13C; U-15N] EBNA2, 1.5 mM Tfb1, 20 mM sodium phosphate, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5 mM [U-100% 15N] EBNA2, 1.5 mM Tfb1, 20 mM sodium phosphate, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5 mM [U-13C; U-15N] EBNA2, 1.5 mM Tfb1, 20 mM sodium phosphate, 1 mM DTT-24, 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.

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EBNA2_EBVB9
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–13; UniProt 453–465

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 2mkr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mkr
Deposition date deposition_date2014-02-12
Structure title titleStructural Characterization of a Complex Between the Acidic Transactivation Domain of EBNA2 and the Tfb1/p62 subunit of TFIIH.
Keywords keywordsEBV, EBNA2, TFIIH, TFB1, ACTIVATION, TRANSCRIPTION, PH DOMAIN, VIRAL PROTEIN-TRANSCRIPTION complex; VIRAL PROTEIN/TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.58
Radius of gyration Rg (electron density) rg_electron15.84
Forward intensity I(0) i01226290000.00
Molecular weight molecular_weight289930.0 kDa
Excluded volume excluded_volume360300 ų
Envelope volume envelope_volume44781 ų
Hydration-shell volume shell_volume19704 ų
Envelope diameter envelope_diameter62.6
Shell Rg shell_rg25.71
Envelope Rg envelope_rg19.65
Shape Rg shape_rg15.83
Total Rg total_rg16.05
Total atoms total_atoms40580
Residues n_residues2560
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 dmax57.0
Rg (real space) rg_real16.54
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.2260e+09
I(0) uncertainty (real space) i0_real_error1.5380e+07
Rg (reciprocal space) rg_reciprocal16.55
I(0) (reciprocal space) i0_reciprocal1226000000.0000
Solution quality estimate total_estimate0.8798
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.243
Kurtosis Kurtosis kurtosis-0.321
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha460000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.985

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_idd2mkra_
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_id2mkrA00
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)