9dil

Cryo-EM structure of VCP/p97 in complex with VCPIP1 (VCIP135)

Method: ELECTRON MICROSCOPY Dmax: 120.7 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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–806 Chain B; UniProt 1–806 Not recorded Deubiquitinating protein VCPIP1 × 1 (Q96JH7) ADP ADENOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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

Deubiquitinating protein VCPIP1

Homo sapiens

UniProt Q96JH7

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 1–1222 Not recorded Transitional endoplasmic reticulum ATPase × 2 (P55072) ADP ADENOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name VCIP1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1222; UniProt 1–1222

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 9dil

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dil
Deposition date deposition_date2024-09-05
Structure title titleCryo-EM structure of VCP/p97 in complex with VCPIP1 (VCIP135)
Keywords keywordsATPase, unfoldase, deubiquitinase, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.14
Radius of gyration Rg (electron density) rg_electron36.47
Forward intensity I(0) i0309904000.00
Molecular weight molecular_weight139360.0 kDa
Excluded volume excluded_volume173600 ų
Envelope volume envelope_volume244780 ų
Hydration-shell volume shell_volume55698 ų
Envelope diameter envelope_diameter131.0
Shell Rg shell_rg42.73
Envelope Rg envelope_rg36.45
Shape Rg shape_rg36.49
Total Rg total_rg36.85
Total atoms total_atoms9783
Residues n_residues1236
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 dmax120.7
Rg (real space) rg_real37.05
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real3.0990e+08
I(0) uncertainty (real space) i0_real_error5.2100e+06
Rg (reciprocal space) rg_reciprocal37.11
I(0) (reciprocal space) i0_reciprocal309900000.0000
Solution quality estimate total_estimate0.8856
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.9
Skewness Skewness skewness0.296
Kurtosis Kurtosis kurtosis-0.329
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33820000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.869

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)