8jg4

Crystal Structure of YAF9A YEATS bound to H3K27cr peptide

Method: X-RAY DIFFRACTION Dmax: 96.5 Å Quality: REASONABLE

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

Transcription initiation factor TFIID subunit 14b

Arabidopsis thaliana

UniProt Q9FH40

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 38–210 Not recorded Histone H3.1 × 1 (P59226) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Tris pH 8.5, 0.2 M Li2SO4, 25% PEG 3350 Resolution 2.30 Å R-free 0.212
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 38–210 Not recorded Histone H3.1 × 1 (P59226) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Tris pH 8.5, 0.2 M Li2SO4, 25% PEG 3350 Resolution 2.30 Å R-free 0.212

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name TA14B_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–189; UniProt 38–210 Author chain B; PDBConstruct 17–189; UniProt 38–210

Histone H3.1

OrganismNot specified

UniProt P59226

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 D; UniProt 25–32 Non-standard monomer:Yes (specific site not provided by mmCIF) Transcription initiation factor TFIID subunit 14b × 1 (Q9FH40) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Tris pH 8.5, 0.2 M Li2SO4, 25% PEG 3350 Resolution 2.30 Å R-free 0.212
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 25–32 Non-standard monomer:Yes (specific site not provided by mmCIF) Transcription initiation factor TFIID subunit 14b × 1 (Q9FH40) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Tris pH 8.5, 0.2 M Li2SO4, 25% PEG 3350 Resolution 2.30 Å R-free 0.212

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.

36 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–8; UniProt 25–32 Author chain D; PDBConstruct 1–8; UniProt 25–32

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 8jg4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8jg4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8jg4
Deposition date deposition_date2023-05-19
最后修订 last_revision2024-05-22
Structure title titleCrystal Structure of YAF9A YEATS bound to H3K27cr peptide
Keywords keywordsYEATS domain, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.08
Radius of gyration Rg (electron density) rg_electron23.19
Forward intensity I(0) i021142100.00
Molecular weight molecular_weight36161.0 kDa
Excluded volume excluded_volume45786 ų
Envelope volume envelope_volume59039 ų
Hydration-shell volume shell_volume22053 ų
Envelope diameter envelope_diameter106.0
Shell Rg shell_rg29.09
Envelope Rg envelope_rg24.35
Shape Rg shape_rg23.18
Total Rg total_rg24.06
Total atoms total_atoms2564
Residues n_residues317
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 dmax96.5
Rg (real space) rg_real24.07
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real2.1140e+07
I(0) uncertainty (real space) i0_real_error3.3340e+05
Rg (reciprocal space) rg_reciprocal24.07
I(0) (reciprocal space) i0_reciprocal21140000.0000
Solution quality estimate total_estimate0.6947
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary31.7
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.173
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8050000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.465; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.646; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)