9j7b

local refinement of FEM1B bound with TOM20(tetramer)

Method: ELECTRON MICROSCOPY Dmax: 157.8 Å Quality: GOOD

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

Protein fem-1 homolog B

Homo sapiens

UniProt Q9UK73

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain A; UniProt 1–627 Chain J; UniProt 1–627 Chain O; UniProt 1–627 Chain P; UniProt 1–627 Not recorded Mitochondrial import receptor subunit TOM20 homolog × 5 (Q15388) Poly-UNK × 1 Poly-UNK × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.12 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.

30 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FEM1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–627; UniProt 1–627 Author chain J; PDBConstruct 1–627; UniProt 1–627 Author chain O; PDBConstruct 1–627; UniProt 1–627 Author chain P; PDBConstruct 1–627; UniProt 1–627

Mitochondrial import receptor subunit TOM20 homolog

Homo sapiens

UniProt Q15388

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain B; UniProt 25–145 Chain C; UniProt 25–145 Chain G; UniProt 25–145 Chain Q; UniProt 25–145 Chain S; UniProt 25–145 Not recorded Protein fem-1 homolog B × 4 (Q9UK73) Poly-UNK × 1 Poly-UNK × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.12 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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOM20_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–121; UniProt 25–145 Author chain C; PDBConstruct 1–121; UniProt 25–145 Author chain G; PDBConstruct 1–121; UniProt 25–145 Author chain Q; PDBConstruct 1–121; UniProt 25–145 Author chain S; PDBConstruct 1–121; UniProt 25–145

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 9j7b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9j7b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9j7b
Deposition date deposition_date2024-08-18
Structure title titlelocal refinement of FEM1B bound with TOM20(tetramer)
Keywords keywordsubiquitination E3 ligase, Cryo-EM, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.10
Radius of gyration Rg (electron density) rg_electron49.63
Forward intensity I(0) i01309360000.00
Molecular weight molecular_weight292670.0 kDa
Excluded volume excluded_volume363430 ų
Envelope volume envelope_volume573370 ų
Hydration-shell volume shell_volume97179 ų
Envelope diameter envelope_diameter160.9
Shell Rg shell_rg54.09
Envelope Rg envelope_rg47.45
Shape Rg shape_rg49.60
Total Rg total_rg49.91
Total atoms total_atoms20578
Residues n_residues2700
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 dmax157.8
Rg (real space) rg_real49.93
Rg uncertainty (real space) rg_real_error1.67
I(0) (real space) i0_real1.3090e+09
I(0) uncertainty (real space) i0_real_error2.6460e+07
Rg (reciprocal space) rg_reciprocal50.24
I(0) (reciprocal space) i0_reciprocal1310000000.0000
Solution quality estimate total_estimate0.8761
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.2
Skewness Skewness skewness0.145
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha65390000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.742

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)