3hqm

Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-CiSBC2

Method: X-RAY DIFFRACTION Dmax: 72.2 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 28–166 Fragment:UNP residues 28-166 Mutation:D140G Protein cubitus interruptus × 1 (P19538) SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.74 Å R-free 0.218
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 28–166 Fragment:UNP residues 28-166 Mutation:D140G Protein cubitus interruptus × 1 (P19538) SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.74 Å R-free 0.218

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 52 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

Protein cubitus interruptus

OrganismNot specified

UniProt P19538

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 C; UniProt 1356–1367 Fragment:UNP residues 1356-1367 Speckle-type POZ protein × 1 (O43791) SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.74 Å R-free 0.218
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1356–1367 Fragment:UNP residues 1356-1367 Speckle-type POZ protein × 1 (O43791) SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.74 Å R-free 0.218

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name CI_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–12; UniProt 1356–1367 Author chain D; PDBConstruct 1–12; UniProt 1356–1367

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 3hqm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3hqm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3hqm
Deposition date deposition_date2009-06-07
Structure title titleStructures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-CiSBC2
Keywords keywords;ubiquitin, E3, SPOP, MATH, Ci, Nucleus, Ubl conjugation pathway, Developmental protein, DNA-binding, Metal-binding, Segmentation polarity protein, Zinc-finger, Protein Binding, LIGASE ;; PROTEIN BINDING, LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.68
Radius of gyration Rg (electron density) rg_electron20.44
Forward intensity I(0) i017589900.00
Molecular weight molecular_weight32184.0 kDa
Excluded volume excluded_volume40504 ų
Envelope volume envelope_volume47490 ų
Hydration-shell volume shell_volume19869 ų
Envelope diameter envelope_diameter72.3
Shell Rg shell_rg26.28
Envelope Rg envelope_rg20.52
Shape Rg shape_rg20.40
Total Rg total_rg21.39
Total atoms total_atoms2258
Residues n_residues281
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 dmax72.2
Rg (real space) rg_real21.68
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.7590e+07
I(0) uncertainty (real space) i0_real_error2.3540e+05
Rg (reciprocal space) rg_reciprocal21.68
I(0) (reciprocal space) i0_reciprocal17590000.0000
Solution quality estimate total_estimate0.8830
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.352
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4338000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3hqma_
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_idd3hqmb_
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_id3hqmA01
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_id3hqmB00
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)