1pfj

Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit

Method: SOLUTION NMR Dmax: 51.9 Å Quality: REASONABLE

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 1–108 Fragment:N-terminal PH/PTB domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.4;293 K;Ionic strength (raw mmCIF value) 20mM;Pressure ambient NMR measurement conditions:pH 7.4;293 K;Ionic strength (raw mmCIF value) 20mM;Pressure ambient NMR measurement conditions:pH 7.4;298 K;Ionic strength (raw mmCIF value) 20mM;Pressure ambient NMR measurement conditions:pH 7.4;293 K;Ionic strength (raw mmCIF value) 20mM;Pressure ambient NMR sample composition:1.5mM P62 U-15N,13C; 20mM deuterated TRIS; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1.2mM P62 U-15N; 20mM deuterated TRIS; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.9mM P62 U-15N; 20mM deuterated TRIS + 26ug C12E6/hexanol; 90% H2O, 10% D2O | 90% H2O, 10% D2O; 26 ug C12E6/hexanol NMR sample composition:1.5mM P62; 20mM deuterated TRIS; 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.

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 1–108; 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 1pfj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1pfj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1pfj
Deposition date deposition_date2003-05-27
Structure title titleSolution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit
Keywords keywordsPH/PTB domain, Structural Proteomics in Europe, SPINE, Structural Genomics, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.43
Radius of gyration Rg (electron density) rg_electron13.77
Forward intensity I(0) i0727102000.00
Molecular weight molecular_weight233520.0 kDa
Excluded volume excluded_volume295220 ų
Envelope volume envelope_volume32233 ų
Hydration-shell volume shell_volume16022 ų
Envelope diameter envelope_diameter56.0
Shell Rg shell_rg23.21
Envelope Rg envelope_rg17.68
Shape Rg shape_rg13.70
Total Rg total_rg14.22
Total atoms total_atoms33497
Residues n_residues2052
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 dmax51.9
Rg (real space) rg_real14.39
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real7.2710e+08
I(0) uncertainty (real space) i0_real_error9.4560e+06
Rg (reciprocal space) rg_reciprocal14.39
I(0) (reciprocal space) i0_reciprocal727100000.0000
Solution quality estimate total_estimate0.7295
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.7
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.175
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha222000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.675; Stabil: 1.000; Sysdev: 0.499; Positv: 1.000; Valcen: 0.958; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1pfja_
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_id1pfjA00
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)