9arr

Crystal structure of AF9 YEATS domain in complex with dicrotonylated at K1007 and K1014 MOZ

Method: X-RAY DIFFRACTION Dmax: 108.8 Å Quality: REASONABLE

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–138 Chain B; UniProt 1–138 Fragment:YEATS domain Histone acetyltransferase KAT6A × 1 (Q92794) LI LITHIUM ION × 2 NO3 NITRATE ION × 4 PEG DI(HYDROXYETHYL)ETHER × 1 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;291 K;0.2 M Lithium nitrate pH 7.1, 20% w/v PEG 3350 Resolution 2.10 Å R-free 0.247

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 38 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 1–138; UniProt 1–138 Author chain B; PDBConstruct 1–138; UniProt 1–138

Histone acetyltransferase KAT6A

OrganismNot specified

UniProt Q92794

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1005–1017 Fragment:residues 1005-1017 (Uniprot numbering) Non-standard monomer:Yes (specific site not provided by mmCIF) Protein AF-9 × 2 (P42568) LI LITHIUM ION × 2 NO3 NITRATE ION × 4 PEG DI(HYDROXYETHYL)ETHER × 1 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;291 K;0.2 M Lithium nitrate pH 7.1, 20% w/v PEG 3350 Resolution 2.10 Å R-free 0.247

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.

20 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAT6A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–13; UniProt 1005–1017

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 9arr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9arr
Deposition date deposition_date2024-02-23
Structure title titleCrystal structure of AF9 YEATS domain in complex with dicrotonylated at K1007 and K1014 MOZ
Keywords keywordsAF9, MOZ, YEATS, crotonylation, Chromatin, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.82
Radius of gyration Rg (electron density) rg_electron30.19
Forward intensity I(0) i019512600.00
Molecular weight molecular_weight34976.0 kDa
Excluded volume excluded_volume44138 ų
Envelope volume envelope_volume57050 ų
Hydration-shell volume shell_volume18010 ų
Envelope diameter envelope_diameter114.0
Shell Rg shell_rg32.47
Envelope Rg envelope_rg30.83
Shape Rg shape_rg30.23
Total Rg total_rg30.31
Total atoms total_atoms2471
Residues n_residues287
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 dmax108.8
Rg (real space) rg_real30.37
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real1.9510e+07
I(0) uncertainty (real space) i0_real_error2.9870e+05
Rg (reciprocal space) rg_reciprocal30.14
I(0) (reciprocal space) i0_reciprocal19510000.0000
Solution quality estimate total_estimate0.6754
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.601
Kurtosis Kurtosis kurtosis-0.506
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4880000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.246; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.078; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)