5c19

p97 variant 2 in the apo state

Method: X-RAY DIFFRACTION Dmax: 160.5 Å Quality: REASONABLE

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 2–806 Chain B; UniProt 2–806 Chain C; UniProt 2–806 Chain D; UniProt 2–806 Chain E; UniProt 2–806 Chain F; UniProt 2–806 Mutation:N750D, R753D, M757D, Q760D SO4 SULFATE ION × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;12% PEG 4000, 0.15 M ammonium sulfate, 0.1 M MES pH 6.5 Resolution 4.20 Å R-free 0.302

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 1–805; UniProt 2–806 Author chain B; PDBConstruct 1–805; UniProt 2–806 Author chain C; PDBConstruct 1–805; UniProt 2–806 Author chain D; PDBConstruct 1–805; UniProt 2–806 Author chain E; PDBConstruct 1–805; UniProt 2–806 Author chain F; PDBConstruct 1–805; UniProt 2–806

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 5c19

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5c19
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5c19
Deposition date deposition_date2015-06-13
Structure title titlep97 variant 2 in the apo state
Keywords keywordsAAA ATPase, ERAD, VCP, CDC48, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier52.34
Radius of gyration Rg (electron density) rg_electron51.99
Forward intensity I(0) i03148350000.00
Molecular weight molecular_weight467000.0 kDa
Excluded volume excluded_volume583870 ų
Envelope volume envelope_volume849240 ų
Hydration-shell volume shell_volume129300 ų
Envelope diameter envelope_diameter169.5
Shell Rg shell_rg60.25
Envelope Rg envelope_rg51.09
Shape Rg shape_rg51.99
Total Rg total_rg52.21
Total atoms total_atoms32773
Residues n_residues4191
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 dmax160.5
Rg (real space) rg_real52.52
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real3.0630e+09
I(0) uncertainty (real space) i0_real_error4.5390e+07
Rg (reciprocal space) rg_reciprocal52.51
I(0) (reciprocal space) i0_reciprocal3150000000.0000
Solution quality estimate total_estimate0.6995
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.2
Skewness Skewness skewness0.212
Kurtosis Kurtosis kurtosis-0.381
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha1.8100
Highest regularization parameter α highest_alpha431300000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 0.923; Sysdev: 0.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.551

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)