7bqz

Crystal Structure of Spindlin1 bound to H3(K4me3-K9me3) peptide

Method: X-RAY DIFFRACTION Dmax: 118.3 Å Quality: GOOD

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

Spindlin-1

Homo sapiens

UniProt Q9Y657

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 45–262 Not recorded H3(K4me3-K9me3) peptide × 1 (Q71DI3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;291 K;2.8M sodium acetate, pH7.0 Resolution 3.10 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 45–262 Not recorded H3(K4me3-K9me3) peptide × 1 (Q71DI3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;291 K;2.8M sodium acetate, pH7.0 Resolution 3.10 Å R-free 0.264
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 45–262 Not recorded H3(K4me3-K9me3) peptide × 1 (Q71DI3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;291 K;2.8M sodium acetate, pH7.0 Resolution 3.10 Å R-free 0.264
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 45–262 Not recorded H3(K4me3-K9me3) peptide × 1 (Q71DI3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;291 K;2.8M sodium acetate, pH7.0 Resolution 3.10 Å R-free 0.264

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.

19 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–220; UniProt 45–262 Author chain C; PDBConstruct 3–220; UniProt 45–262 Author chain E; PDBConstruct 3–220; UniProt 45–262 Author chain G; PDBConstruct 3–220; UniProt 45–262

H3(K4me3-K9me3) peptide

OrganismNot specified

UniProt Q71DI3

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 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) Spindlin-1 × 1 (Q9Y657) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;291 K;2.8M sodium acetate, pH7.0 Resolution 3.10 Å R-free 0.264
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) Spindlin-1 × 1 (Q9Y657) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;291 K;2.8M sodium acetate, pH7.0 Resolution 3.10 Å R-free 0.264
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) Spindlin-1 × 1 (Q9Y657) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;291 K;2.8M sodium acetate, pH7.0 Resolution 3.10 Å R-free 0.264
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) Spindlin-1 × 1 (Q9Y657) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;291 K;2.8M sodium acetate, pH7.0 Resolution 3.10 Å R-free 0.264

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.

139 other PDB entries and 154 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 2–16 Author chain D; PDBConstruct 1–15; UniProt 2–16 Author chain F; PDBConstruct 1–15; UniProt 2–16 Author chain H; 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 7bqz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7bqz
Deposition date deposition_date2020-03-26
Structure title titleCrystal Structure of Spindlin1 bound to H3(K4me3-K9me3) peptide
Keywords keywordsSpin/Ssty repeat, 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_guinier35.15
Radius of gyration Rg (electron density) rg_electron34.11
Forward intensity I(0) i0156137000.00
Molecular weight molecular_weight100320.0 kDa
Excluded volume excluded_volume125720 ų
Envelope volume envelope_volume178340 ų
Hydration-shell volume shell_volume43224 ų
Envelope diameter envelope_diameter120.1
Shell Rg shell_rg41.38
Envelope Rg envelope_rg33.23
Shape Rg shape_rg34.13
Total Rg total_rg34.60
Total atoms total_atoms7064
Residues n_residues867
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 dmax118.3
Rg (real space) rg_real35.03
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real1.5610e+08
I(0) uncertainty (real space) i0_real_error2.5990e+06
Rg (reciprocal space) rg_reciprocal35.10
I(0) (reciprocal space) i0_reciprocal156100000.0000
Solution quality estimate total_estimate0.8933
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.3
Skewness Skewness skewness0.145
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35830000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)