4hs2

Crystal Structure of the Human SPOP C-terminal Domain

Method: X-RAY DIFFRACTION Dmax: 37.1 Å Quality: GOOD

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

Speckle-type POZ protein

Homo sapiens

UniProt O43791

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 270–374 Fragment:C-terminal domain (UNP residues 270-374) Mutation:L273D, L282D, L285K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;291 K;26% PEG 1500, 7% isopropanol, 0.1M CaCl2, 0.1M imidazole pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.53 Å R-free 0.151

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.

34 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPOP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–110; UniProt 270–374

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 4hs2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4hs2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4hs2
Deposition date deposition_date2012-10-29
Structure title titleCrystal Structure of the Human SPOP C-terminal Domain
Keywords keywordsprotein interaction domain, Oligomerisation, 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_guinier12.26
Radius of gyration Rg (electron density) rg_electron10.69
Forward intensity I(0) i01139110.00
Molecular weight molecular_weight6927.0 kDa
Excluded volume excluded_volume8645 ų
Envelope volume envelope_volume9573 ų
Hydration-shell volume shell_volume7854 ų
Envelope diameter envelope_diameter33.9
Shell Rg shell_rg16.05
Envelope Rg envelope_rg11.07
Shape Rg shape_rg10.69
Total Rg total_rg12.21
Total atoms total_atoms489
Residues n_residues64
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 dmax37.1
Rg (real space) rg_real12.17
Rg uncertainty (real space) rg_real_error0.16
I(0) (real space) i0_real1.1390e+06
I(0) uncertainty (real space) i0_real_error1.1450e+04
Rg (reciprocal space) rg_reciprocal12.17
I(0) (reciprocal space) i0_reciprocal1139000.0000
Solution quality estimate total_estimate0.8959
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.9
Skewness Skewness skewness0.054
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha139500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4hs2A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily420

8. Citations (1)

9. Files and Curves (10)