9y03

Cryo-EM structure of human VCP/p97-R89W mutant bound to ADP

Method: ELECTRON MICROSCOPY Dmax: 140.8 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 Mutation:R89W ADP ADENOSINE-5'-DIPHOSPHATE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 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 17–822; UniProt 1–806 Author chain B; PDBConstruct 17–822; UniProt 1–806 Author chain C; PDBConstruct 17–822; UniProt 1–806 Author chain D; PDBConstruct 17–822; UniProt 1–806 Author chain E; PDBConstruct 17–822; UniProt 1–806 Author chain F; PDBConstruct 17–822; 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 9y03

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9y03
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9y03
Deposition date deposition_date2025-08-28
Structure title titleCryo-EM structure of human VCP/p97-R89W mutant bound to ADP
Keywords keywordsAAA ATPase, Unfoldase, ERAD, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.94
Radius of gyration Rg (electron density) rg_electron45.25
Forward intensity I(0) i01989330000.00
Molecular weight molecular_weight366380.0 kDa
Excluded volume excluded_volume457130 ų
Envelope volume envelope_volume620220 ų
Hydration-shell volume shell_volume107100 ų
Envelope diameter envelope_diameter143.1
Shell Rg shell_rg55.14
Envelope Rg envelope_rg44.36
Shape Rg shape_rg45.25
Total Rg total_rg45.61
Total atoms total_atoms25692
Residues n_residues3264
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 dmax140.8
Rg (real space) rg_real45.57
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.9890e+09
I(0) uncertainty (real space) i0_real_error3.3530e+07
Rg (reciprocal space) rg_reciprocal45.94
I(0) (reciprocal space) i0_reciprocal1990000000.0000
Solution quality estimate total_estimate0.8902
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.1
Skewness Skewness skewness0.056
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha473200000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)