29hi

Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO22 SCF ubiquition ligase in complex with NSD2 via UNC10415667

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

F-box only protein 22

Homo sapiens

UniProt Q8NEZ5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 Histone-lysine N-methyltransferase NSD2 × 1 (O96028) S-phase kinase-associated protein 1 × 1 (P63208) Cullin-1 × 1 (Q13616) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ;4-[[cyclopropyl-[(~{Z})-2-methyl-4-(5-oxidanylidene-2~{H}-1,4-oxazin-3-yl)but-3-enoyl]amino]methyl]-~{N}-[3-[2-[[4-(hydroxymethyl)phenyl]carbonyl-methyl-amino]ethyl]phenyl]benzamide ; × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FBX22_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–403; UniProt 1–403

Histone-lysine N-methyltransferase NSD2

Homo sapiens

UniProt O96028

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 F-box only protein 22 × 1 (Q8NEZ5) S-phase kinase-associated protein 1 × 1 (P63208) Cullin-1 × 1 (Q13616) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ;4-[[cyclopropyl-[(~{Z})-2-methyl-4-(5-oxidanylidene-2~{H}-1,4-oxazin-3-yl)but-3-enoyl]amino]methyl]-~{N}-[3-[2-[[4-(hydroxymethyl)phenyl]carbonyl-methyl-amino]ethyl]phenyl]benzamide ; × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NSD2_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1365; UniProt 1–1365

S-phase kinase-associated protein 1

Homo sapiens

UniProt P63208

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 F-box only protein 22 × 1 (Q8NEZ5) Histone-lysine N-methyltransferase NSD2 × 1 (O96028) Cullin-1 × 1 (Q13616) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ;4-[[cyclopropyl-[(~{Z})-2-methyl-4-(5-oxidanylidene-2~{H}-1,4-oxazin-3-yl)but-3-enoyl]amino]methyl]-~{N}-[3-[2-[[4-(hydroxymethyl)phenyl]carbonyl-methyl-amino]ethyl]phenyl]benzamide ; × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name SKP1_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–163; UniProt 1–163

Cullin-1

Homo sapiens

UniProt Q13616

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 5 F-box only protein 22 × 1 (Q8NEZ5) Histone-lysine N-methyltransferase NSD2 × 1 (O96028) S-phase kinase-associated protein 1 × 1 (P63208) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ;4-[[cyclopropyl-[(~{Z})-2-methyl-4-(5-oxidanylidene-2~{H}-1,4-oxazin-3-yl)but-3-enoyl]amino]methyl]-~{N}-[3-[2-[[4-(hydroxymethyl)phenyl]carbonyl-methyl-amino]ethyl]phenyl]benzamide ; × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CUL1_HUMAN
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–776; UniProt 1–776

E3 ubiquitin-protein ligase RBX1

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 5 F-box only protein 22 × 1 (Q8NEZ5) Histone-lysine N-methyltransferase NSD2 × 1 (O96028) S-phase kinase-associated protein 1 × 1 (P63208) Cullin-1 × 1 (Q13616) ;4-[[cyclopropyl-[(~{Z})-2-methyl-4-(5-oxidanylidene-2~{H}-1,4-oxazin-3-yl)but-3-enoyl]amino]methyl]-~{N}-[3-[2-[[4-(hydroxymethyl)phenyl]carbonyl-methyl-amino]ethyl]phenyl]benzamide ; × 1 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 5
Chains and sequence ranges Author chain E; PDBConstruct 1–108; UniProt 1–108

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_id29hi
Deposition date deposition_date2026-03-11
Structure title titleCryo-EM structure of the CUL1-RBX1-SKP1-FBXO22 SCF ubiquition ligase in complex with NSD2 via UNC10415667
Keywords keywords;Ubiquitin Ligase, Targeted protein degradation, cullin-RING ligase, SKP1 CUL1 F box SCF, Nuclear receptor binding SET domain-containing 2 NSD2, LIGASE ;; LIGASE
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.

29hi__assembly_1__model_1

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

Download this curve (.dat)

29hi__assembly_1__model_1 | I(q)

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

29hi__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)53.15 Å
Rg (electron density)53.21 Å
Total Rg53.41 Å
Atom count12383
Residues1540
Excluded volume220550 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 29hi__assembly_1__model_1 pentameric (5) 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 (6)

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7. Citations (2)