8hrz

Crystal structure of the p97-N/D1 hexamer in complex with six p47-UBX domains

Method: X-RAY DIFFRACTION Dmax: 212.4 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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 21–458 Chain B; UniProt 21–458 Chain C; UniProt 21–458 Chain D; UniProt 21–458 Chain E; UniProt 21–458 Chain F; UniProt 21–458 Chain G; UniProt 21–458 Chain H; UniProt 21–458 Chain I; UniProt 21–458 Chain J; UniProt 21–458 Chain K; UniProt 21–458 Chain L; UniProt 21–458 Mutation:E294A, K295A NSFL1 cofactor p47 × 12 (Q9UNZ2) ADP ADENOSINE-5'-DIPHOSPHATE × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;14% PEG 3350, 0.2M ammonium citrate tribasic (pH 7), 0.01M hexamine cobalt (III) chloride Resolution 2.70 Å R-free 0.256

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 1–438; UniProt 21–458 Author chain B; PDBConstruct 1–438; UniProt 21–458 Author chain C; PDBConstruct 1–438; UniProt 21–458 Author chain D; PDBConstruct 1–438; UniProt 21–458 Author chain E; PDBConstruct 1–438; UniProt 21–458 Author chain F; PDBConstruct 1–438; UniProt 21–458 Author chain G; PDBConstruct 1–438; UniProt 21–458 Author chain H; PDBConstruct 1–438; UniProt 21–458 Author chain I; PDBConstruct 1–438; UniProt 21–458 Author chain J; PDBConstruct 1–438; UniProt 21–458 Author chain K; PDBConstruct 1–438; UniProt 21–458 Author chain L; PDBConstruct 1–438; UniProt 21–458

NSFL1 cofactor p47

Homo sapiens

UniProt Q9UNZ2

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain M; UniProt 287–370 Chain N; UniProt 287–370 Chain O; UniProt 287–370 Chain P; UniProt 287–370 Chain Q; UniProt 287–370 Chain R; UniProt 287–370 Chain S; UniProt 287–370 Chain T; UniProt 287–370 Chain U; UniProt 287–370 Chain V; UniProt 287–370 Chain W; UniProt 287–370 Chain X; UniProt 287–370 Not recorded Transitional endoplasmic reticulum ATPase × 12 (P55072) ADP ADENOSINE-5'-DIPHOSPHATE × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;14% PEG 3350, 0.2M ammonium citrate tribasic (pH 7), 0.01M hexamine cobalt (III) chloride Resolution 2.70 Å R-free 0.256

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSF1C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 2–85; UniProt 287–370 Author chain N; PDBConstruct 2–85; UniProt 287–370 Author chain O; PDBConstruct 2–85; UniProt 287–370 Author chain P; PDBConstruct 2–85; UniProt 287–370 Author chain Q; PDBConstruct 2–85; UniProt 287–370 Author chain R; PDBConstruct 2–85; UniProt 287–370 Author chain S; PDBConstruct 2–85; UniProt 287–370 Author chain T; PDBConstruct 2–85; UniProt 287–370 Author chain U; PDBConstruct 2–85; UniProt 287–370 Author chain V; PDBConstruct 2–85; UniProt 287–370 Author chain W; PDBConstruct 2–85; UniProt 287–370 Author chain X; PDBConstruct 2–85; UniProt 287–370

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 8hrz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8hrz
Deposition date deposition_date2022-12-16
Structure title titleCrystal structure of the p97-N/D1 hexamer in complex with six p47-UBX domains
Keywords keywordsPROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier64.23
Radius of gyration Rg (electron density) rg_electron64.09
Forward intensity I(0) i06950790000.00
Molecular weight molecular_weight699910.0 kDa
Excluded volume excluded_volume875610 ų
Envelope volume envelope_volume1382400 ų
Hydration-shell volume shell_volume173670 ų
Envelope diameter envelope_diameter205.6
Shell Rg shell_rg70.24
Envelope Rg envelope_rg62.05
Shape Rg shape_rg64.09
Total Rg total_rg64.20
Total atoms total_atoms49084
Residues n_residues6252
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 dmax212.4
Rg (real space) rg_real63.84
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real6.9510e+09
I(0) uncertainty (real space) i0_real_error1.2430e+08
Rg (reciprocal space) rg_reciprocal64.53
I(0) (reciprocal space) i0_reciprocal6959000000.0000
Solution quality estimate total_estimate0.8538
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.7
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha739800000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.792; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.777

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)