9t2z

Spindlin 1 with crystallization epitope mutations H127D:L128D:T131R

Method: X-RAY DIFFRACTION Dmax: 58.2 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 49–262 Mutation:H127D:L128D:T131R EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.15 K;0.2M ammonium sulfate 25% PEG3350 0.1M HEPES pH 7.5 Resolution 1.87 Å R-free 0.288

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 2–215; UniProt 49–262

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 9t2z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t2z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9t2z
Deposition date deposition_date2025-10-24
最后修订 last_revision2025-11-26
Structure title titleSpindlin 1 with crystallization epitope mutations H127D:L128D:T131R
Keywords keywordsCrystal epitopes, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.35
Radius of gyration Rg (electron density) rg_electron17.82
Forward intensity I(0) i010023700.00
Molecular weight molecular_weight23443.0 kDa
Excluded volume excluded_volume29351 ų
Envelope volume envelope_volume36375 ų
Hydration-shell volume shell_volume17157 ų
Envelope diameter envelope_diameter58.2
Shell Rg shell_rg23.85
Envelope Rg envelope_rg18.17
Shape Rg shape_rg17.80
Total Rg total_rg18.90
Total atoms total_atoms1653
Residues n_residues208
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 dmax58.2
Rg (real space) rg_real19.21
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.0020e+07
I(0) uncertainty (real space) i0_real_error1.1820e+05
Rg (reciprocal space) rg_reciprocal19.23
I(0) (reciprocal space) i0_reciprocal10020000.0000
Solution quality estimate total_estimate0.9104
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.071
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2620000.0000
Real-space data points n_real_points72
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: 0.992; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)