4w5a

Complex structure of ATRX ADD bound to H3K9me3S10ph peptide

Method: X-RAY DIFFRACTION Dmax: 93.8 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:UNP residues 167-289 Mutation:K251R, F284Y Peptide from Histone H3.3 × 1 (P84243) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;13-20% PEG 4000, 0.1 M MES, 3 mM MgCl2 Resolution 2.60 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 167–289 Fragment:UNP residues 167-289 Mutation:K251R, F284Y Peptide from Histone H3.3 × 1 (P84243) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;13-20% PEG 4000, 0.1 M MES, 3 mM MgCl2 Resolution 2.60 Å R-free 0.260
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 167–289 Fragment:UNP residues 167-289 Mutation:K251R, F284Y Peptide from Histone H3.3 × 1 (P84243) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;13-20% PEG 4000, 0.1 M MES, 3 mM MgCl2 Resolution 2.60 Å R-free 0.260

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 16 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 Author chain B; PDBConstruct 7–129; UniProt 167–289 Author chain E; PDBConstruct 7–129; UniProt 167–289

Peptide from 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 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;277 K;13-20% PEG 4000, 0.1 M MES, 3 mM MgCl2 Resolution 2.60 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 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;277 K;13-20% PEG 4000, 0.1 M MES, 3 mM MgCl2 Resolution 2.60 Å R-free 0.260
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 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;277 K;13-20% PEG 4000, 0.1 M MES, 3 mM MgCl2 Resolution 2.60 Å R-free 0.260

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 121 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 Author chain D; PDBConstruct 1–15; UniProt 2–16 Author chain F; 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 4w5a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4w5a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4w5a
Deposition date deposition_date2014-08-17
Structure title titleComplex structure of ATRX ADD bound to H3K9me3S10ph peptide
Keywords keywordsEpigenetic regulation, Complex, Transcription, Mitosis, HYDROLASE-STRUCTURAL PROTEIN complex; HYDROLASE/STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.25
Radius of gyration Rg (electron density) rg_electron27.87
Forward intensity I(0) i043862900.00
Molecular weight molecular_weight46837.0 kDa
Excluded volume excluded_volume56615 ų
Envelope volume envelope_volume74882 ų
Hydration-shell volume shell_volume24396 ų
Envelope diameter envelope_diameter94.2
Shell Rg shell_rg32.91
Envelope Rg envelope_rg27.67
Shape Rg shape_rg27.90
Total Rg total_rg28.28
Total atoms total_atoms3210
Residues n_residues396
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 dmax93.8
Rg (real space) rg_real28.56
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real4.3860e+07
I(0) uncertainty (real space) i0_real_error6.9760e+05
Rg (reciprocal space) rg_reciprocal28.47
I(0) (reciprocal space) i0_reciprocal43860000.0000
Solution quality estimate total_estimate0.8359
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.504
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha8023000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.787; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.707; Smooth: 0.794

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)