11ve

Cryo-EM structure of substrate engaged p97-Ufd1-NPL4-Faf1 complex (State1)

Method: ELECTRON MICROSCOPY Dmax: 186.9 Å Quality: REASONABLE

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–608 Not recorded FAS-associated factor 1 × 2 (Q9UNN5) Ubiquitin recognition factor in ER-associated degradation protein 1 × 1 (Q92890) Transitional endoplasmic reticulum ATPase × 6 (P55072) ZN ZINC ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.85 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 1–608; UniProt 1–608

FAS-associated factor 1

Homo sapiens

UniProt Q9UNN5

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain M; UniProt 481–650 Chain O; UniProt 481–650 Not recorded Nuclear protein localization protein 4 homolog × 1 (Q8TAT6) Ubiquitin recognition factor in ER-associated degradation protein 1 × 1 (Q92890) Transitional endoplasmic reticulum ATPase × 6 (P55072) ZN ZINC ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.85 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.

15 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FAF1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 4–173; UniProt 481–650 Author chain O; PDBConstruct 4–173; UniProt 481–650

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain P; UniProt 1–307 Not recorded Nuclear protein localization protein 4 homolog × 1 (Q8TAT6) FAS-associated factor 1 × 2 (Q9UNN5) Transitional endoplasmic reticulum ATPase × 6 (P55072) ZN ZINC ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.85 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

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 × 10 PDB declaration: decameric(10) 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 Nuclear protein localization protein 4 homolog × 1 (Q8TAT6) FAS-associated factor 1 × 2 (Q9UNN5) Ubiquitin recognition factor in ER-associated degradation protein 1 × 1 (Q92890) ZN ZINC ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.85 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 4
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 11ve

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id11ve
Deposition date deposition_date2026-03-13
Structure title titleCryo-EM structure of substrate engaged p97-Ufd1-NPL4-Faf1 complex (State1)
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_guinier56.58
Radius of gyration Rg (electron density) rg_electron56.07
Forward intensity I(0) i03789840000.00
Molecular weight molecular_weight503330.0 kDa
Excluded volume excluded_volume624450 ų
Envelope volume envelope_volume978050 ų
Hydration-shell volume shell_volume139730 ų
Envelope diameter envelope_diameter189.4
Shell Rg shell_rg62.96
Envelope Rg envelope_rg55.64
Shape Rg shape_rg56.14
Total Rg total_rg56.02
Total atoms total_atoms35382
Residues n_residues4663
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 dmax186.9
Rg (real space) rg_real56.35
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real3.7900e+09
I(0) uncertainty (real space) i0_real_error7.6360e+07
Rg (reciprocal space) rg_reciprocal56.76
I(0) (reciprocal space) i0_reciprocal3792000000.0000
Solution quality estimate total_estimate0.6403
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.4
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha451100000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.966; Smooth: 0.805

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)