2dii

Solution structure of the BSD domain of human TFIIH basal transcription factor complex p62 subunit

Method: SOLUTION NMR Dmax: 53.2 Å Quality: GOOD

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 103–150 Fragment:BSD domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;296 K;Ionic strength (raw mmCIF value) 120;Pressure ambient NMR sample composition:1.07mM BSD domain U-15N,13C; 20mM d-Tris HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 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.

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 1
Chains and sequence ranges Author chain A; PDBConstruct 8–55; UniProt 103–150

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 2dii

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2dii
Deposition date deposition_date2006-03-30
Structure title titleSolution structure of the BSD domain of human TFIIH basal transcription factor complex p62 subunit
Keywords keywords;BTF2-p62, General transcription factor IIH polypeptide 1, Nuclear protein, Transcription regulation, structural genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.84
Radius of gyration Rg (electron density) rg_electron13.42
Forward intensity I(0) i0275014000.00
Molecular weight molecular_weight135130.0 kDa
Excluded volume excluded_volume167610 ų
Envelope volume envelope_volume29903 ų
Hydration-shell volume shell_volume14997 ų
Envelope diameter envelope_diameter58.1
Shell Rg shell_rg23.01
Envelope Rg envelope_rg17.83
Shape Rg shape_rg13.38
Total Rg total_rg13.85
Total atoms total_atoms18880
Residues n_residues1220
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 dmax53.2
Rg (real space) rg_real13.85
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real2.7500e+08
I(0) uncertainty (real space) i0_real_error3.7530e+06
Rg (reciprocal space) rg_reciprocal13.85
I(0) (reciprocal space) i0_reciprocal275000000.0000
Solution quality estimate total_estimate0.7896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary16.2
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.070
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64970.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.468; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.866; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2diia1
Class classa — All alpha proteins
Fold Fold folda.240 — BSD domain-like
Superfamily Superfamily superfamilya.240.1 — BSD domain-like
Family Family familya.240.1.1 — BSD domain
Domain ID domain_idd2diia2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2diia3
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_id2diiA01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily1200

8. Citations (1)

9. Files and Curves (10)