3hsv

Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-MacroH2ASBCpep2

Method: X-RAY DIFFRACTION Dmax: 80.8 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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 28–166 Chain B; UniProt 28–166 Mutation:D140G Core histone macro-H2A.1 × 1 (O75367) ZN ZINC ION × 3 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.43 Å R-free 0.206

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 7–145; UniProt 28–166 Author chain B; PDBConstruct 7–145; UniProt 28–166

Core histone macro-H2A.1

Homo sapiens

UniProt O75367

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain M; UniProt 171–186 Non-standard monomer:Yes (specific site not provided by mmCIF) Speckle-type POZ protein × 2 (O43791) ZN ZINC ION × 3 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.43 Å R-free 0.206

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.

6 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AY_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 1–16; UniProt 171–186

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 3hsv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3hsv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3hsv
Deposition date deposition_date2009-06-10
Structure title titleStructures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-MacroH2ASBCpep2
Keywords keywords;ubiquitin, E3, SPOP, MacroH2A, Nucleus, Ubl conjugation pathway, Alternative splicing, Chromatin regulator, Chromosomal protein, DNA-binding, Isopeptide bond, Methylation, Nucleosome core, Phosphoprotein, Ubl conjugation, ligase, protein binding ;; protein binding, ligase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.26
Radius of gyration Rg (electron density) rg_electron22.40
Forward intensity I(0) i016913500.00
Molecular weight molecular_weight31866.0 kDa
Excluded volume excluded_volume40174 ų
Envelope volume envelope_volume48207 ų
Hydration-shell volume shell_volume18869 ų
Envelope diameter envelope_diameter80.9
Shell Rg shell_rg28.01
Envelope Rg envelope_rg22.55
Shape Rg shape_rg22.38
Total Rg total_rg23.23
Total atoms total_atoms2231
Residues n_residues276
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 dmax80.8
Rg (real space) rg_real23.38
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.6910e+07
I(0) uncertainty (real space) i0_real_error2.5240e+05
Rg (reciprocal space) rg_reciprocal23.36
I(0) (reciprocal space) i0_reciprocal16910000.0000
Solution quality estimate total_estimate0.8521
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.461
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4022000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.829; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3hsva_
Class classb — All beta proteins
Fold Fold foldb.8 — TRAF domain-like
Superfamily Superfamily superfamilyb.8.1 — TRAF domain-like
Family Family familyb.8.1.1 — MATH domain
Domain ID domain_idd3hsvb_
Class classb — All beta proteins
Fold Fold foldb.8 — TRAF domain-like
Superfamily Superfamily superfamilyb.8.1 — TRAF domain-like
Family Family familyb.8.1.1 — MATH domain

CATH v4.4 (2 domains)

Domain ID domain_id3hsvA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Domain ID domain_id3hsvB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A

8. Citations (1)

9. Files and Curves (10)