9mpr

Cryo-EM structure of three VCPIP1 VCPIDs bound to VCP

Method: ELECTRON MICROSCOPY Dmax: 148.3 Å Quality: GOOD

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

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain G; UniProt 1–1222 Chain H; UniProt 1–1222 Chain I; UniProt 1–1222 Not recorded Transitional endoplasmic reticulum ATPase × 6 (P55072) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 1
Chains and sequence ranges Author chain G; PDBConstruct 29–1250; UniProt 1–1222 Author chain H; PDBConstruct 29–1250; UniProt 1–1222 Author chain I; PDBConstruct 29–1250; UniProt 1–1222

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 × 9 PDB declaration: nonameric(9) 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 Deubiquitinating protein VCPIP1 × 3 (Q96JH7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 2
Chains and sequence ranges Author chain A; PDBConstruct 27–832; UniProt 1–806 Author chain B; PDBConstruct 27–832; UniProt 1–806 Author chain C; PDBConstruct 27–832; UniProt 1–806 Author chain D; PDBConstruct 27–832; UniProt 1–806 Author chain E; PDBConstruct 27–832; UniProt 1–806 Author chain F; PDBConstruct 27–832; 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 9mpr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mpr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9mpr
Deposition date deposition_date2024-12-31
最后修订 last_revision2025-10-15
Structure title titleCryo-EM structure of three VCPIP1 VCPIDs bound to VCP
Keywords keywords;double-ring hexameric complex, valosin containing protein, ATPase, VCP, mammalian, DUB, deubiquitinase, deubiquitinating enzyme, VCIP135, p97, VCPIP1, hydrolase, VCPID ;; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.03
Radius of gyration Rg (electron density) rg_electron46.07
Forward intensity I(0) i02264770000.00
Molecular weight molecular_weight396820.0 kDa
Excluded volume excluded_volume497220 ų
Envelope volume envelope_volume680760 ų
Hydration-shell volume shell_volume114940 ų
Envelope diameter envelope_diameter158.4
Shell Rg shell_rg56.76
Envelope Rg envelope_rg45.07
Shape Rg shape_rg46.08
Total Rg total_rg46.43
Total atoms total_atoms55729
Residues n_residues3563
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 dmax148.3
Rg (real space) rg_real46.62
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real2.2650e+09
I(0) uncertainty (real space) i0_real_error4.1220e+07
Rg (reciprocal space) rg_reciprocal47.03
I(0) (reciprocal space) i0_reciprocal2266000000.0000
Solution quality estimate total_estimate0.8812
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary143.9
Skewness Skewness skewness0.062
Kurtosis Kurtosis kurtosis-0.488
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha852600000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)