11sy

Cryo-EM structure of substrate engaged p97-Ufd1-NPL4-Faf1 complex (NPL4 focused)

Method: ELECTRON MICROSCOPY Dmax: 108.8 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Nuclear protein localization protein 4 homolog

Homo sapiens

UniProt Q8TAT6

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 2–608 Not recorded Ubiquitin × 4 (P0CG48) Ubiquitin recognition factor in ER-associated degradation protein 1 × 1 (Q92890) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;50 mM HEPES, pH 7.6, 150 mM KCl, 5 mM MgCl2, 2 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.28 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NPL4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; PDBConstruct 5–611; UniProt 2–608

Ubiquitin

Homo sapiens

UniProt P0CG48

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain H; UniProt 1–76 Chain I; UniProt 1–76 Chain J; UniProt 1–76 Chain K; UniProt 1–76 Not recorded Nuclear protein localization protein 4 homolog × 1 (Q8TAT6) Ubiquitin recognition factor in ER-associated degradation protein 1 × 1 (Q92890) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;50 mM HEPES, pH 7.6, 150 mM KCl, 5 mM MgCl2, 2 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.28 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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–76; UniProt 1–76 Author chain I; PDBConstruct 1–76; UniProt 1–76 Author chain J; PDBConstruct 1–76; UniProt 1–76 Author chain K; PDBConstruct 1–76; UniProt 1–76

Ubiquitin recognition factor in ER-associated degradation protein 1

Homo sapiens

UniProt Q92890

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain P; UniProt 1–307 Not recorded Nuclear protein localization protein 4 homolog × 1 (Q8TAT6) Ubiquitin × 4 (P0CG48) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;50 mM HEPES, pH 7.6, 150 mM KCl, 5 mM MgCl2, 2 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.28 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UFD1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–307; UniProt 1–307

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 11sy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11sy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id11sy
Deposition date deposition_date2026-03-11
Structure title titleCryo-EM structure of substrate engaged p97-Ufd1-NPL4-Faf1 complex (NPL4 focused)
Keywords keywordsERAD, ubiquitin, AAA+ ATPase, unfoldase, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.75
Radius of gyration Rg (electron density) rg_electron31.97
Forward intensity I(0) i0114838000.00
Molecular weight molecular_weight85547.0 kDa
Excluded volume excluded_volume107310 ų
Envelope volume envelope_volume143950 ų
Hydration-shell volume shell_volume38126 ų
Envelope diameter envelope_diameter114.2
Shell Rg shell_rg38.34
Envelope Rg envelope_rg32.16
Shape Rg shape_rg31.90
Total Rg total_rg32.75
Total atoms total_atoms6018
Residues n_residues755
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 dmax108.8
Rg (real space) rg_real32.75
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real1.1480e+08
I(0) uncertainty (real space) i0_real_error1.9240e+06
Rg (reciprocal space) rg_reciprocal32.75
I(0) (reciprocal space) i0_reciprocal114800000.0000
Solution quality estimate total_estimate0.8881
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.3
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15500000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.888

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)