8fco

Cryo-EM structure of p97:UBXD1 meta state

Method: ELECTRON MICROSCOPY Dmax: 199.1 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 × 8 PDB declaration: octameric(8) 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 UBX domain-containing protein 6 × 2 (Q9BZV1) ADP ADENOSINE-5'-DIPHOSPHATE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 10 sec, blot time 3 sec, blot force 0 Resolution 3.31 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

UBX domain-containing protein 6

Homo sapiens

UniProt Q9BZV1

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 1–441 Chain H; UniProt 1–441 Not recorded Transitional endoplasmic reticulum ATPase × 6 (P55072) ADP ADENOSINE-5'-DIPHOSPHATE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 10 sec, blot time 3 sec, blot force 0 Resolution 3.31 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBXN6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–441; UniProt 1–441 Author chain H; PDBConstruct 1–441; UniProt 1–441

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 8fco

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8fco
Deposition date deposition_date2022-12-01
Structure title titleCryo-EM structure of p97:UBXD1 meta state
Keywords keywordsAAA+, chaperone, hydrolase; CHAPERONE, HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.42
Radius of gyration Rg (electron density) rg_electron59.67
Forward intensity I(0) i04561510000.00
Molecular weight molecular_weight563910.0 kDa
Excluded volume excluded_volume704840 ų
Envelope volume envelope_volume1070100 ų
Hydration-shell volume shell_volume145700 ų
Envelope diameter envelope_diameter216.0
Shell Rg shell_rg63.89
Envelope Rg envelope_rg59.96
Shape Rg shape_rg59.71
Total Rg total_rg59.62
Total atoms total_atoms39569
Residues n_residues4999
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 dmax199.1
Rg (real space) rg_real59.42
Rg uncertainty (real space) rg_real_error1.84
I(0) (real space) i0_real4.5610e+09
I(0) uncertainty (real space) i0_real_error1.0110e+08
Rg (reciprocal space) rg_reciprocal59.41
I(0) (reciprocal space) i0_reciprocal4561000000.0000
Solution quality estimate total_estimate0.8491
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary68.9
Skewness Skewness skewness0.430
Kurtosis Kurtosis kurtosis-0.035
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha405800000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.667

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)