1h3o

Crystal Structure of the Human TAF4-TAF12 (TAFII135-TAFII20) Complex

Method: X-RAY DIFFRACTION Dmax: 61.5 Å Quality: EXCELLENT

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

TRANSCRIPTION INITIATION FACTOR TFIID 135 KDA SUBUNIT

HOMO SAPIENS

UniProt O00268

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 870–943 Fragment:HISTONE FOLD DOMAIN, RESIDUES 870-943 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) TRANSCRIPTION INITIATION FACTOR TFIID 20/15 KDA SUBUNITS × 1 (Q16514) X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.25;pH 5.25 Resolution 2.30 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 870–943 Fragment:HISTONE FOLD DOMAIN, RESIDUES 870-943 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) TRANSCRIPTION INITIATION FACTOR TFIID 20/15 KDA SUBUNITS × 1 (Q16514) X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.25;pH 5.25 Resolution 2.30 Å R-free 0.272

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.

30 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name T2D3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–75; UniProt 870–943 Author chain C; PDBConstruct 2–75; UniProt 870–943

TRANSCRIPTION INITIATION FACTOR TFIID 20/15 KDA SUBUNITS

HOMO SAPIENS

UniProt Q16514

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 57–128 Fragment:HISTONE FOLD DOMAIN, RESIDUES 57-128 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) TRANSCRIPTION INITIATION FACTOR TFIID 135 KDA SUBUNIT × 1 (O00268) X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.25;pH 5.25 Resolution 2.30 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 57–128 Fragment:HISTONE FOLD DOMAIN, RESIDUES 57-128 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) TRANSCRIPTION INITIATION FACTOR TFIID 135 KDA SUBUNIT × 1 (O00268) X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.25;pH 5.25 Resolution 2.30 Å R-free 0.272

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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name T2DA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–76; UniProt 57–128 Author chain D; PDBConstruct 5–76; UniProt 57–128

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 1h3o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1h3o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1h3o
Deposition date deposition_date2002-09-12
Structure title titleCrystal Structure of the Human TAF4-TAF12 (TAFII135-TAFII20) Complex
Keywords keywords;TRANSCRIPTION/TBP-ASSOCIATED FACTORS, TBP-ASSOCIATED FACTORS, TFIID, RNA POLYMERASE II TRANSCRIPTION, HISTONE FOLD DOMAINS, NUCLEAR PROTEIN, TRANSCRIPTION-TBP-ASSOCIATED FACTORS complex ;; TRANSCRIPTION/TBP-ASSOCIATED FACTORS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.66
Radius of gyration Rg (electron density) rg_electron19.58
Forward intensity I(0) i015288300.00
Molecular weight molecular_weight29078.0 kDa
Excluded volume excluded_volume36109 ų
Envelope volume envelope_volume42528 ų
Hydration-shell volume shell_volume18229 ų
Envelope diameter envelope_diameter61.9
Shell Rg shell_rg25.71
Envelope Rg envelope_rg19.57
Shape Rg shape_rg19.62
Total Rg total_rg20.29
Total atoms total_atoms2014
Residues n_residues240
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 dmax61.5
Rg (real space) rg_real20.55
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.5290e+07
I(0) uncertainty (real space) i0_real_error1.7040e+05
Rg (reciprocal space) rg_reciprocal20.57
I(0) (reciprocal space) i0_reciprocal15290000.0000
Solution quality estimate total_estimate0.9150
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.082
Kurtosis Kurtosis kurtosis-0.692
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4325000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.970; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1h3oa_
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_idd1h3ob1
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_idd1h3ob2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1h3oc_
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_idd1h3od1
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_idd1h3od2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id1h3oA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id1h3oB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id1h3oC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id1h3oD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (2)

9. Files and Curves (10)