8y1u

Crystal structure of ASB7-Elongin B/C bound to the LZTS1-degron

Method: X-RAY DIFFRACTION Dmax: 112.1 Å Quality: REASONABLE

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

Ankyrin repeat and SOCS box protein 7

Homo sapiens

UniProt Q9H672

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 11–318 Not recorded Peptide from Leucine zipper putative tumor suppressor 1 × 1 (Q9Y250) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M DL-Malic acid pH7.0, 10% w/v polyethylene glycol 3350 Resolution 2.41 Å R-free 0.243

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 ASB7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–309; UniProt 11–318

Peptide from Leucine zipper putative tumor suppressor 1

OrganismNot specified

UniProt Q9Y250

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 346–368 Not recorded Ankyrin repeat and SOCS box protein 7 × 1 (Q9H672) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M DL-Malic acid pH7.0, 10% w/v polyethylene glycol 3350 Resolution 2.41 Å R-free 0.243

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 LZTS1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–23; UniProt 346–368

Elongin-B

Homo sapiens

UniProt Q15370

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–104 Not recorded Ankyrin repeat and SOCS box protein 7 × 1 (Q9H672) Peptide from Leucine zipper putative tumor suppressor 1 × 1 (Q9Y250) Elongin-C × 1 (Q15369) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M DL-Malic acid pH7.0, 10% w/v polyethylene glycol 3350 Resolution 2.41 Å R-free 0.243

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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–104; UniProt 1–104

Elongin-C

Homo sapiens

UniProt Q15369

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 17–112 Not recorded Ankyrin repeat and SOCS box protein 7 × 1 (Q9H672) Peptide from Leucine zipper putative tumor suppressor 1 × 1 (Q9Y250) Elongin-B × 1 (Q15370) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M DL-Malic acid pH7.0, 10% w/v polyethylene glycol 3350 Resolution 2.41 Å R-free 0.243

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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–96; UniProt 17–112

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 8y1u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8y1u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8y1u
Deposition date deposition_date2024-01-25
最后修订 last_revision2024-12-04
Structure title titleCrystal structure of ASB7-Elongin B/C bound to the LZTS1-degron
Keywords keywordsubiquitin ligase, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.47
Radius of gyration Rg (electron density) rg_electron29.10
Forward intensity I(0) i036066200.00
Molecular weight molecular_weight44081.0 kDa
Excluded volume excluded_volume54074 ų
Envelope volume envelope_volume74878 ų
Hydration-shell volume shell_volume23252 ų
Envelope diameter envelope_diameter115.4
Shell Rg shell_rg33.00
Envelope Rg envelope_rg30.77
Shape Rg shape_rg29.16
Total Rg total_rg29.30
Total atoms total_atoms3106
Residues n_residues423
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 dmax112.1
Rg (real space) rg_real29.91
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real3.6070e+07
I(0) uncertainty (real space) i0_real_error5.9960e+05
Rg (reciprocal space) rg_reciprocal29.73
I(0) (reciprocal space) i0_reciprocal36060000.0000
Solution quality estimate total_estimate0.7378
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.682
Kurtosis Kurtosis kurtosis-0.045
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13630000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.433; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.326; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)