9im4

Crystal Structure of AF9 YEATS domain F28R mutant in complex with histone H3K9la

Method: X-RAY DIFFRACTION Dmax: 77.2 Å Quality: GOOD

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

Protein AF-9

Homo sapiens

UniProt P42568

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 1–138 Mutation:F28R Histone H3.3C × 1 (Q6NXT2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;2.1M DL Malic acid pH7.0 Resolution 2.79 Å R-free 0.315
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–138 Mutation:F28R Histone H3.3C × 1 (Q6NXT2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;2.1M DL Malic acid pH7.0 Resolution 2.79 Å R-free 0.315

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.

24 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AF9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–158; UniProt 1–138 Author chain B; PDBConstruct 21–158; UniProt 1–138

Histone H3.3C

OrganismNot specified

UniProt Q6NXT2

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 P; UniProt 2–11 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein AF-9 × 1 (P42568) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;2.1M DL Malic acid pH7.0 Resolution 2.79 Å R-free 0.315
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–11 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein AF-9 × 1 (P42568) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;2.1M DL Malic acid pH7.0 Resolution 2.79 Å R-free 0.315

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.

22 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–10; UniProt 2–11 Author chain P; PDBConstruct 1–10; UniProt 2–11

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 9im4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9im4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9im4
Deposition date deposition_date2024-07-02
最后修订 last_revision2025-07-09
Structure title titleCrystal Structure of AF9 YEATS domain F28R mutant in complex with histone H3K9la
Keywords keywordsYEATS domain, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.94
Radius of gyration Rg (electron density) rg_electron22.98
Forward intensity I(0) i040031900.00
Molecular weight molecular_weight32515.0 kDa
Excluded volume excluded_volume31337 ų
Envelope volume envelope_volume57929 ų
Hydration-shell volume shell_volume21337 ų
Envelope diameter envelope_diameter81.9
Shell Rg shell_rg29.27
Envelope Rg envelope_rg22.88
Shape Rg shape_rg22.93
Total Rg total_rg23.67
Total atoms total_atoms2473
Residues n_residues294
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 dmax77.2
Rg (real space) rg_real23.83
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real4.0030e+07
I(0) uncertainty (real space) i0_real_error5.3220e+05
Rg (reciprocal space) rg_reciprocal23.86
I(0) (reciprocal space) i0_reciprocal40030000.0000
Solution quality estimate total_estimate0.8988
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.0
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.632
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6962000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)