3ql9

Monoclinic complex structure of ATRX ADD bound to histone H3K9me3 peptide

Method: X-RAY DIFFRACTION Dmax: 56.7 Å Quality: GOOD

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

Transcriptional regulator ATRX

Homo sapiens

UniProt P46100

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 167–289 Fragment:N-terminal ADD domain, UNP residues 167-289 Mutation:K251R, F284Y peptide of Histone H3.3 × 1 (P84243) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.1;277 K;14% PEG 4000, 0.1M MES, 0.2 M KCL, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 0.93 Å R-free 0.131

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATRX_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–129; UniProt 167–289

peptide of Histone H3.3

OrganismNot specified

UniProt P84243

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 C; UniProt 2–16 Fragment:K9 trimethylated H3 N-terminal fragment, UNP residues 2-16 Non-standard monomer:Yes (specific site not provided by mmCIF) Transcriptional regulator ATRX × 1 (P46100) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.1;277 K;14% PEG 4000, 0.1M MES, 0.2 M KCL, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 0.93 Å R-free 0.131

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.

94 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–15; UniProt 2–16

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 3ql9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ql9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ql9
Deposition date deposition_date2011-02-02
Structure title titleMonoclinic complex structure of ATRX ADD bound to histone H3K9me3 peptide
Keywords keywords;zinc finger, transcription, histone, lysine trimethylation, nuclear protein, HISTONE-BINDING PROTEIN, TRANSCRIPTION-STRUCTURAL PROTEIN complex ;; TRANSCRIPTION/STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.09
Radius of gyration Rg (electron density) rg_electron14.97
Forward intensity I(0) i05693860.00
Molecular weight molecular_weight15822.0 kDa
Excluded volume excluded_volume19145 ų
Envelope volume envelope_volume21490 ų
Hydration-shell volume shell_volume12390 ų
Envelope diameter envelope_diameter55.7
Shell Rg shell_rg20.54
Envelope Rg envelope_rg15.54
Shape Rg shape_rg15.03
Total Rg total_rg15.78
Total atoms total_atoms1086
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 dmax56.7
Rg (real space) rg_real16.08
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real5.6940e+06
I(0) uncertainty (real space) i0_real_error6.0010e+04
Rg (reciprocal space) rg_reciprocal16.08
I(0) (reciprocal space) i0_reciprocal5694000.0000
Solution quality estimate total_estimate0.8456
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.188
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1130000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.696; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)