9j79

Cryo-EM structure of CRL2-FEM1B bound with TOM20(tetramer)

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Cullin-2

Homo sapiens

UniProt Q13617

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 19 Elongin-C × 2 (Q15369) Elongin-B × 2 (Q15370) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein fem-1 homolog B × 4 (Q9UK73) Mitochondrial import receptor subunit TOM20 homolog × 4 (Q15388) Poly-UNK × 2 Poly-UNK × 1 ZINC ION × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CUL2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 22–750; UniProt 2–745 Author chain K; PDBConstruct 22–750; UniProt 2–745

Elongin-C

Homo sapiens

UniProt Q15369

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 19 Cullin-2 × 2 (Q13617) Elongin-B × 2 (Q15370) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein fem-1 homolog B × 4 (Q9UK73) Mitochondrial import receptor subunit TOM20 homolog × 4 (Q15388) Poly-UNK × 2 Poly-UNK × 1 ZINC ION × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–96; UniProt 17–112 Author chain L; PDBConstruct 1–96; UniProt 17–112

Elongin-B

Homo sapiens

UniProt Q15370

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 19 Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein fem-1 homolog B × 4 (Q9UK73) Mitochondrial import receptor subunit TOM20 homolog × 4 (Q15388) Poly-UNK × 2 Poly-UNK × 1 ZINC ION × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 4–121; UniProt 1–118 Author chain M; PDBConstruct 4–121; UniProt 1–118

E3 ubiquitin-protein ligase RBX1, N-terminally processed

Homo sapiens

UniProt P62877

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 19 Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) Elongin-B × 2 (Q15370) Protein fem-1 homolog B × 4 (Q9UK73) Mitochondrial import receptor subunit TOM20 homolog × 4 (Q15388) Poly-UNK × 2 Poly-UNK × 1 ZINC ION × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform —
PDB entities 4
Chains and sequence ranges Author chain I; PDBConstruct 4–96; UniProt 16–108 Author chain N; PDBConstruct 4–96; UniProt 16–108

Protein fem-1 homolog B

Homo sapiens

UniProt Q9UK73

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 19 Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) Elongin-B × 2 (Q15370) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Mitochondrial import receptor subunit TOM20 homolog × 4 (Q15388) Poly-UNK × 2 Poly-UNK × 1 ZINC ION × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FEM1B_HUMAN
Isoform —
PDB entities 5
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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 19 Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) Elongin-B × 2 (Q15370) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein fem-1 homolog B × 4 (Q9UK73) Poly-UNK × 2 Poly-UNK × 1 ZINC ION × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TOM20_HUMAN
Isoform —
PDB entities 6
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 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id9j79
Deposition date deposition_date2024-08-18
Structure title titleCryo-EM structure of CRL2-FEM1B bound with TOM20(tetramer)
Keywords keywordsubiquitination E3 ligase, Cryo-EM, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9j79__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9j79__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9j79__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)68.49 Å
Rg (electron density)68.28 Å
Total Rg68.29 Å
Atom count36721
Residues4678
Excluded volume652130 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9j79__assembly_1__model_1 19-meric (19) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (9)

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7. Citations (1)