7yta

crystal structure of NtAGDP3 AGD1-2 in complex with an H3K9me2 peptide

Method: X-RAY DIFFRACTION Dmax: 99.0 Å Quality: GOOD

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

AGDP3 AGD1-2

Nicotiana tabacum

UniProt A0A1S4CD95

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 1–150 Mutation:L12I,T13A,A16S,V17I,L110M,E137Q H3(1-15)K9me2 peptide × 1 (P59226) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;25% PEG 1500, 0.1 M sodium chloride and 0.1 M bis-Tris propane, pH 9.0 Resolution 2.31 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–150 Mutation:L12I,T13A,A16S,V17I,L110M,E137Q H3(1-15)K9me2 peptide × 1 (P59226) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;25% PEG 1500, 0.1 M sodium chloride and 0.1 M bis-Tris propane, pH 9.0 Resolution 2.31 Å R-free 0.271
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–150 Mutation:L12I,T13A,A16S,V17I,L110M,E137Q H3(1-15)K9me2 peptide × 1 (P59226) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;25% PEG 1500, 0.1 M sodium chloride and 0.1 M bis-Tris propane, pH 9.0 Resolution 2.31 Å R-free 0.271

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A1S4CD95_TOBAC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–151; UniProt 1–150 Author chain B; PDBConstruct 2–151; UniProt 1–150 Author chain C; PDBConstruct 2–151; UniProt 1–150

H3(1-15)K9me2 peptide

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) AGDP3 AGD1-2 × 1 (A0A1S4CD95) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;25% PEG 1500, 0.1 M sodium chloride and 0.1 M bis-Tris propane, pH 9.0 Resolution 2.31 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Q; UniProt 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) AGDP3 AGD1-2 × 1 (A0A1S4CD95) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;25% PEG 1500, 0.1 M sodium chloride and 0.1 M bis-Tris propane, pH 9.0 Resolution 2.31 Å R-free 0.271
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain R; UniProt 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) AGDP3 AGD1-2 × 1 (A0A1S4CD95) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;25% PEG 1500, 0.1 M sodium chloride and 0.1 M bis-Tris propane, pH 9.0 Resolution 2.31 Å R-free 0.271

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 45 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 Author chain Q; PDBConstruct 1–15; UniProt 2–16 Author chain R; 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 7yta

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7yta
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7yta
Deposition date deposition_date2022-08-13
Structure title titlecrystal structure of NtAGDP3 AGD1-2 in complex with an H3K9me2 peptide
Keywords keywordsAGENET domain, ROS1, H3K9me2 binding, 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_guinier28.29
Radius of gyration Rg (electron density) rg_electron27.94
Forward intensity I(0) i040860100.00
Molecular weight molecular_weight50847.0 kDa
Excluded volume excluded_volume64134 ų
Envelope volume envelope_volume84234 ų
Hydration-shell volume shell_volume26917 ų
Envelope diameter envelope_diameter105.8
Shell Rg shell_rg33.08
Envelope Rg envelope_rg28.08
Shape Rg shape_rg27.89
Total Rg total_rg28.66
Total atoms total_atoms3607
Residues n_residues440
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 dmax99.0
Rg (real space) rg_real28.48
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real4.0860e+07
I(0) uncertainty (real space) i0_real_error6.2370e+05
Rg (reciprocal space) rg_reciprocal28.43
I(0) (reciprocal space) i0_reciprocal40860000.0000
Solution quality estimate total_estimate0.8575
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.480
Kurtosis Kurtosis kurtosis-0.284
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7181000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.784; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.815; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)