9eqm

Crystal structure of pVHL:EloB:EloC in complex with MP-1-21

Method: X-RAY DIFFRACTION Dmax: 86.3 Å Quality: REASONABLE

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–104 Not recorded Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1H9F (2S,4R)-1-[(2R)-2-[(1-fluoranylcyclopropyl)carbonylamino]-3-methyl-3-[[trans-4-(morpholin-4-ylmethyl)cyclohexyl]methylsulfanyl]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.285 M sodium acetate, 0.1M Bis-Tris pH 5.5, and 5.9% PEG3350 Resolution 2.19 Å R-free 0.264

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 1
Chains and sequence ranges Author chain A; 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1H9F (2S,4R)-1-[(2R)-2-[(1-fluoranylcyclopropyl)carbonylamino]-3-methyl-3-[[trans-4-(morpholin-4-ylmethyl)cyclohexyl]methylsulfanyl]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.285 M sodium acetate, 0.1M Bis-Tris pH 5.5, and 5.9% PEG3350 Resolution 2.19 Å R-free 0.264

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 2
Chains and sequence ranges Author chain B; PDBConstruct 2–97; UniProt 17–112

von Hippel-Lindau disease tumor suppressor

Homo sapiens

UniProt P40337

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 C; UniProt 54–213 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) A1H9F (2S,4R)-1-[(2R)-2-[(1-fluoranylcyclopropyl)carbonylamino]-3-methyl-3-[[trans-4-(morpholin-4-ylmethyl)cyclohexyl]methylsulfanyl]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.285 M sodium acetate, 0.1M Bis-Tris pH 5.5, and 5.9% PEG3350 Resolution 2.19 Å R-free 0.264

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.

141 other PDB entries and 363 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VHL_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 3–162; UniProt 54–213

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 9eqm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9eqm
Deposition date deposition_date2024-03-21
最后修订 last_revision2024-08-28
Structure title titleCrystal structure of pVHL:EloB:EloC in complex with MP-1-21
Keywords keywordsE3 ligase, von Hippel-Lindau tumor-suppressor protein, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.82
Radius of gyration Rg (electron density) rg_electron23.93
Forward intensity I(0) i024739800.00
Molecular weight molecular_weight38304.0 kDa
Excluded volume excluded_volume48061 ų
Envelope volume envelope_volume58495 ų
Hydration-shell volume shell_volume21493 ų
Envelope diameter envelope_diameter89.5
Shell Rg shell_rg29.73
Envelope Rg envelope_rg24.00
Shape Rg shape_rg23.96
Total Rg total_rg24.57
Total atoms total_atoms5288
Residues n_residues341
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 dmax86.3
Rg (real space) rg_real24.92
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real2.4740e+07
I(0) uncertainty (real space) i0_real_error3.8960e+05
Rg (reciprocal space) rg_reciprocal24.90
I(0) (reciprocal space) i0_reciprocal24740000.0000
Solution quality estimate total_estimate0.6319
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.404
Kurtosis Kurtosis kurtosis-0.375
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4263000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 0.996; Sysdev: 0.338; Positv: 1.000; Valcen: 0.814; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)