1bh8

HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE

Method: X-RAY DIFFRACTION Dmax: 55.3 Å Quality: GOOD

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

TAFII18

Homo sapiens

UniProt Q15543

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 31–75 Fragment:RESIDUES 31 - 75 TAFII28 × 1 (Q15544) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 3.00 Å R-free 0.282

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 TAF13_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–45; UniProt 31–75

TAFII28

Homo sapiens

UniProt Q15544

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 113–201 Fragment:RESIDUES 113 - 201 TAFII18 × 1 (Q15543) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 3.00 Å R-free 0.282

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 TAF11_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–89; UniProt 113–201

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 1bh8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bh8
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1bh8
Deposition date deposition_date1998-06-16
Structure title titleHTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE
Keywords keywordsHTAFII28, HISTONE FOLD, TATA BINDING PROTEIN, TRANSCRIPTION REGULATION COMPLEX; TRANSCRIPTION REGULATION COMPLEX
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.73
Radius of gyration Rg (electron density) rg_electron15.49
Forward intensity I(0) i04595050.00
Molecular weight molecular_weight15367.0 kDa
Excluded volume excluded_volume19289 ų
Envelope volume envelope_volume22027 ų
Hydration-shell volume shell_volume12517 ų
Envelope diameter envelope_diameter54.0
Shell Rg shell_rg20.74
Envelope Rg envelope_rg15.83
Shape Rg shape_rg15.48
Total Rg total_rg16.56
Total atoms total_atoms1074
Residues n_residues134
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 dmax55.3
Rg (real space) rg_real16.70
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real4.5950e+06
I(0) uncertainty (real space) i0_real_error5.0850e+04
Rg (reciprocal space) rg_reciprocal16.71
I(0) (reciprocal space) i0_reciprocal4595000.0000
Solution quality estimate total_estimate0.8916
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.365
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha730600.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bh8a_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.3 — TBP-associated factors, TAFs
Domain ID domain_idd1bh8b_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.3 — TBP-associated factors, TAFs

CATH v4.4 (2 domains)

Domain ID domain_id1bh8A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id1bh8B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)