6lqe

Crystal structure of Arabidopsis ARID5 PHD finger in complex with H3K4me3 peptide

Method: X-RAY DIFFRACTION Dmax: 41.0 Å Quality: GOOD

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

AT-rich interactive domain-containing protein 4

Arabidopsis thaliana

UniProt Q6NQ79

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 673–747 Not recorded 15-mer peptide from Histone H3.2 × 1 (P59226) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;298 K;0.1 M sodium acetate, pH 4.6, 30% PEG 300 Resolution 1.90 Å R-free 0.241

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARID4_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–76; UniProt 673–747

15-mer peptide from Histone H3.2

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 P; UniProt 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) AT-rich interactive domain-containing protein 4 × 1 (Q6NQ79) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;298 K;0.1 M sodium acetate, pH 4.6, 30% PEG 300 Resolution 1.90 Å R-free 0.241

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 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; 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 6lqe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6lqe
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6lqe
Deposition date deposition_date2020-01-13
Structure title titleCrystal structure of Arabidopsis ARID5 PHD finger in complex with H3K4me3 peptide
Keywords keywordsARID5, PHD finger, histone, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier12.10
Radius of gyration Rg (electron density) rg_electron10.85
Forward intensity I(0) i01377000.00
Molecular weight molecular_weight7025.0 kDa
Excluded volume excluded_volume8410 ų
Envelope volume envelope_volume9504 ų
Hydration-shell volume shell_volume7738 ų
Envelope diameter envelope_diameter39.2
Shell Rg shell_rg16.12
Envelope Rg envelope_rg11.36
Shape Rg shape_rg10.82
Total Rg total_rg12.23
Total atoms total_atoms480
Residues n_residues62
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 dmax41.0
Rg (real space) rg_real12.03
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real1.3770e+06
I(0) uncertainty (real space) i0_real_error1.4050e+04
Rg (reciprocal space) rg_reciprocal12.04
I(0) (reciprocal space) i0_reciprocal1377000.0000
Solution quality estimate total_estimate0.8709
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.6
Skewness Skewness skewness0.167
Kurtosis Kurtosis kurtosis-0.269
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha143700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)