4iur

crystal structure of SHH1 SAWADEE domain in complex with H3K9me3 peptide

Method: X-RAY DIFFRACTION Dmax: 86.0 Å Quality: GOOD

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

SHH1 SAWADEE

Arabidopsis thaliana

UniProt Q9XI47

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 B; UniProt 125–258 Fragment:SHH1 SAWADEE domain (unp residues 125-258) Histone H3.2, H3(1-15)K9me3 × 1 (P59226) ZN ZINC ION × 1 CVM CYMAL-4 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.2 M NH4F, 20% PEG 3350, 7.6 mM 4-Cyclohexyl-1-Butyl-D-Maltoside , VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.50 Å R-free 0.256
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 125–258 Fragment:SHH1 SAWADEE domain (unp residues 125-258) ZN ZINC ION × 1 CVM CYMAL-4 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.2 M NH4F, 20% PEG 3350, 7.6 mM 4-Cyclohexyl-1-Butyl-D-Maltoside , VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.50 Å R-free 0.256

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.

5 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9XI47_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–135; UniProt 125–258 Author chain B; PDBConstruct 2–135; UniProt 125–258

Histone H3.2, H3(1-15)K9me3

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 C; UniProt 2–16 Fragment:H3(1-15) K9me3 peptide (unp residues 2-16) Non-standard monomer:Yes (specific site not provided by mmCIF) SHH1 SAWADEE × 1 (Q9XI47) ZN ZINC ION × 1 CVM CYMAL-4 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.2 M NH4F, 20% PEG 3350, 7.6 mM 4-Cyclohexyl-1-Butyl-D-Maltoside , VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.50 Å R-free 0.256

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 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 4iur

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4iur
Deposition date deposition_date2013-01-21
Structure title titlecrystal structure of SHH1 SAWADEE domain in complex with H3K9me3 peptide
Keywords keywordstandem tudor, zinc finger, H3K9me3, mediate interaction, histone, methylation, 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_guinier24.08
Radius of gyration Rg (electron density) rg_electron23.50
Forward intensity I(0) i020446100.00
Molecular weight molecular_weight32712.0 kDa
Excluded volume excluded_volume40304 ų
Envelope volume envelope_volume52940 ų
Hydration-shell volume shell_volume20091 ų
Envelope diameter envelope_diameter89.3
Shell Rg shell_rg28.87
Envelope Rg envelope_rg23.49
Shape Rg shape_rg23.47
Total Rg total_rg24.30
Total atoms total_atoms2293
Residues n_residues273
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 dmax86.0
Rg (real space) rg_real24.24
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real2.0450e+07
I(0) uncertainty (real space) i0_real_error2.8050e+05
Rg (reciprocal space) rg_reciprocal24.20
I(0) (reciprocal space) i0_reciprocal20450000.0000
Solution quality estimate total_estimate0.8517
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.506
Kurtosis Kurtosis kurtosis-0.094
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2411000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.765; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.790; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4iurA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id4iurA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily140
Domain ID domain_id4iurB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id4iurB02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily140

8. Citations (1)

9. Files and Curves (10)