6lqf

Crystal structure of Arabidopsis ARID5 ARID-PHD cassette in complex with H3K4me3 peptide and DNA

Method: X-RAY DIFFRACTION Dmax: 62.5 Å Quality: EXCELLENT

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–DNA Heteromer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 545–747 Not recorded 15-mer peptide from Histone H3.2 × 1 (P59226) ;DNA (5'-D(*TP*TP*TP*AP*GP*AP*TP*CP*TP*AP*AP*A)-3') ; × 2 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5;298 K;0.1 M sodium acetate, pH 5.0, 15% MPD Resolution 1.50 Å R-free 0.192

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 2–204; UniProt 545–747

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–DNA Heteromer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain P; UniProt 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) AT-rich interactive domain-containing protein 4 × 1 (Q6NQ79) ;DNA (5'-D(*TP*TP*TP*AP*GP*AP*TP*CP*TP*AP*AP*A)-3') ; × 2 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5;298 K;0.1 M sodium acetate, pH 5.0, 15% MPD Resolution 1.50 Å R-free 0.192

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 6lqf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6lqf
Deposition date deposition_date2020-01-13
Structure title titleCrystal structure of Arabidopsis ARID5 ARID-PHD cassette in complex with H3K4me3 peptide and DNA
Keywords keywordsARID5, PHD finger, ARID domain, 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_guinier20.00
Radius of gyration Rg (electron density) rg_electron18.99
Forward intensity I(0) i019641600.00
Molecular weight molecular_weight27984.0 kDa
Excluded volume excluded_volume32489 ų
Envelope volume envelope_volume39937 ų
Hydration-shell volume shell_volume17998 ų
Envelope diameter envelope_diameter62.9
Shell Rg shell_rg24.75
Envelope Rg envelope_rg19.15
Shape Rg shape_rg18.89
Total Rg total_rg19.93
Total atoms total_atoms1925
Residues n_residues204
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 dmax62.5
Rg (real space) rg_real19.93
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.9640e+07
I(0) uncertainty (real space) i0_real_error2.5150e+05
Rg (reciprocal space) rg_reciprocal19.95
I(0) (reciprocal space) i0_reciprocal19640000.0000
Solution quality estimate total_estimate0.9111
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.537
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2869000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6lqfA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily60 — ARID DNA-binding domain

8. Citations (1)

9. Files and Curves (10)