8rsc

p97 (VCP) mutant - F539A

Method: ELECTRON MICROSCOPY Dmax: 177.2 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 × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;pre-blotting incubation time of 20 secounds and blot for 3.5 seconds with -1 blot force 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 8rsc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rsc
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8rsc
Deposition date deposition_date2024-01-24
Structure title titlep97 (VCP) mutant - F539A
Keywords keywordsHexameric complex, ATPase, Unfoldase, Protein Quality Control, Segregase, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.67
Radius of gyration Rg (electron density) rg_electron53.23
Forward intensity I(0) i03253420000.00
Molecular weight molecular_weight453050.0 kDa
Excluded volume excluded_volume556660 ų
Envelope volume envelope_volume930270 ų
Hydration-shell volume shell_volume136500 ų
Envelope diameter envelope_diameter169.4
Shell Rg shell_rg62.03
Envelope Rg envelope_rg53.00
Shape Rg shape_rg53.36
Total Rg total_rg53.04
Total atoms total_atoms31874
Residues n_residues4457
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 dmax177.2
Rg (real space) rg_real54.41
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real3.2530e+09
I(0) uncertainty (real space) i0_real_error5.6640e+07
Rg (reciprocal space) rg_reciprocal54.88
I(0) (reciprocal space) i0_reciprocal3256000000.0000
Solution quality estimate total_estimate0.8779
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.2
Skewness Skewness skewness0.162
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha566200000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)