8yka

Cryo-EM structure of P97-VCPIP1 complex

Method: ELECTRON MICROSCOPY Dmax: 231.9 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 12–775 Chain B; UniProt 12–775 Chain C; UniProt 12–775 Chain D; UniProt 12–775 Chain E; UniProt 12–775 Chain F; UniProt 12–775 Not recorded Deubiquitinating protein VCPIP1 × 3 (Q96JH7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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 1–764; UniProt 12–775 Author chain B; PDBConstruct 1–764; UniProt 12–775 Author chain C; PDBConstruct 1–764; UniProt 12–775 Author chain D; PDBConstruct 1–764; UniProt 12–775 Author chain E; PDBConstruct 1–764; UniProt 12–775 Author chain F; PDBConstruct 1–764; UniProt 12–775

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 1; UniProt 105–673 Chain 2; UniProt 105–673 Chain 3; UniProt 105–673 Not recorded Transitional endoplasmic reticulum ATPase × 6 (P55072) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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 1; PDBConstruct 1–569; UniProt 105–673 Author chain 2; PDBConstruct 1–569; UniProt 105–673 Author chain 3; PDBConstruct 1–569; UniProt 105–673

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 8yka

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8yka
Deposition date deposition_date2024-03-04
Structure title titleCryo-EM structure of P97-VCPIP1 complex
Keywords keywordsP97/VCP ATPase; Golgi apparatus; membrane fusion; VCPIP1, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.40
Radius of gyration Rg (electron density) rg_electron68.41
Forward intensity I(0) i06951640000.00
Molecular weight molecular_weight702210.0 kDa
Excluded volume excluded_volume878730 ų
Envelope volume envelope_volume1437000 ų
Hydration-shell volume shell_volume175460 ų
Envelope diameter envelope_diameter228.8
Shell Rg shell_rg70.09
Envelope Rg envelope_rg66.77
Shape Rg shape_rg68.42
Total Rg total_rg68.41
Total atoms total_atoms49338
Residues n_residues6291
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 dmax231.9
Rg (real space) rg_real68.30
Rg uncertainty (real space) rg_real_error2.51
I(0) (real space) i0_real6.9520e+09
I(0) uncertainty (real space) i0_real_error1.4080e+08
Rg (reciprocal space) rg_reciprocal68.70
I(0) (reciprocal space) i0_reciprocal6956000000.0000
Solution quality estimate total_estimate0.8560
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary80.7
Skewness Skewness skewness0.272
Kurtosis Kurtosis kurtosis-0.318
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha631000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.663

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)