8vov

Structure of VCP in complex with an ATPase activator and ADP (D2 domains only, hexameric form)

Method: ELECTRON MICROSCOPY Dmax: 143.1 Å Quality: GOOD

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

Transitional endoplasmic reticulum ATPase

Homo sapiens

UniProt P55072

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–806 Chain B; UniProt 1–806 Chain C; UniProt 1–806 Chain D; UniProt 1–806 Chain E; UniProt 1–806 Chain F; UniProt 1–806 Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 A1AC1 (3R)-N-[2-(ethylsulfanyl)phenyl]-3-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM K.HEPES pH 7.5, 25 mM KCl, 2.5 mM MgCl2, 2.5 mM GSH, 0.5% DMSO, 0.01% FOM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 Å

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.

143 other PDB entries and 156 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TERA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–806; UniProt 1–806 Author chain B; PDBConstruct 1–806; UniProt 1–806 Author chain C; PDBConstruct 1–806; UniProt 1–806 Author chain D; PDBConstruct 1–806; UniProt 1–806 Author chain E; PDBConstruct 1–806; UniProt 1–806 Author chain F; PDBConstruct 1–806; UniProt 1–806

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 8vov

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vov
Deposition date deposition_date2024-01-16
最后修订 last_revision2024-06-19
Structure title titleStructure of VCP in complex with an ATPase activator and ADP (D2 domains only, hexameric form)
Keywords keywordsactivator, complex, ATPase, AAA protein, HYDROLASE, HYDROLASE-ACTIVATOR complex; HYDROLASE/ACTIVATOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.02
Radius of gyration Rg (electron density) rg_electron43.40
Forward intensity I(0) i0596808000.00
Molecular weight molecular_weight199400.0 kDa
Excluded volume excluded_volume248980 ų
Envelope volume envelope_volume362960 ų
Hydration-shell volume shell_volume66943 ų
Envelope diameter envelope_diameter148.4
Shell Rg shell_rg50.58
Envelope Rg envelope_rg42.91
Shape Rg shape_rg43.41
Total Rg total_rg43.72
Total atoms total_atoms13998
Residues n_residues1734
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 dmax143.1
Rg (real space) rg_real43.91
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real5.9680e+08
I(0) uncertainty (real space) i0_real_error1.1330e+07
Rg (reciprocal space) rg_reciprocal44.02
I(0) (reciprocal space) i0_reciprocal596900000.0000
Solution quality estimate total_estimate0.8975
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.645
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha220000000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.917

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)