7cna

Crystal structure of Spindlin1/C11orf84 complex bound to histone H3K4me3K9me3 peptide

Method: X-RAY DIFFRACTION Dmax: 84.0 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 51–262 Chain D; UniProt 51–262 Not recorded Spindlin interactor and repressor of chromatin-binding protein × 2 (Q9BUA3) ALA-ARG-THR-M3L-GLN-THR-ALA-ARG-M3L-SER-THR × 1 ALA-ARG-THR-M3L-GLN-THR-ALA-ARG-M3L-SER-GLY × 1 BEN BENZAMIDINE × 6 CL CHLORIDE ION × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M sodium cacodylate pH 6.5, 35% PEG3350, 5% glycerol, 2% Benzamidine hydrochloride Resolution 1.60 Å R-free 0.201

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 34 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 1–212; UniProt 51–262 Author chain D; PDBConstruct 1–212; UniProt 51–262

Spindlin interactor and repressor of chromatin-binding protein

Homo sapiens

UniProt Q9BUA3

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 254–283 Chain E; UniProt 254–283 Not recorded Spindlin-1 × 2 (Q9Y657) ALA-ARG-THR-M3L-GLN-THR-ALA-ARG-M3L-SER-THR × 1 ALA-ARG-THR-M3L-GLN-THR-ALA-ARG-M3L-SER-GLY × 1 BEN BENZAMIDINE × 6 CL CHLORIDE ION × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M sodium cacodylate pH 6.5, 35% PEG3350, 5% glycerol, 2% Benzamidine hydrochloride Resolution 1.60 Å R-free 0.201

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPNDC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–30; UniProt 254–283 Author chain E; PDBConstruct 1–30; UniProt 254–283

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 7cna

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7cna
Deposition date deposition_date2020-07-30
Structure title titleCrystal structure of Spindlin1/C11orf84 complex bound to histone H3K4me3K9me3 peptide
Keywords keywordsepigenetic reader, protein binding; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.86
Radius of gyration Rg (electron density) rg_electron24.43
Forward intensity I(0) i051264200.00
Molecular weight molecular_weight56066.0 kDa
Excluded volume excluded_volume70354 ų
Envelope volume envelope_volume87755 ų
Hydration-shell volume shell_volume29665 ų
Envelope diameter envelope_diameter89.2
Shell Rg shell_rg31.75
Envelope Rg envelope_rg24.35
Shape Rg shape_rg24.43
Total Rg total_rg25.28
Total atoms total_atoms3954
Residues n_residues487
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 dmax84.0
Rg (real space) rg_real25.75
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real5.1260e+07
I(0) uncertainty (real space) i0_real_error7.3260e+05
Rg (reciprocal space) rg_reciprocal25.79
I(0) (reciprocal space) i0_reciprocal51270000.0000
Solution quality estimate total_estimate0.8105
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary34.4
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.334
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19660000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)