4f52

Structure of a Glomulin-RBX1-CUL1 complex

Method: X-RAY DIFFRACTION
▼

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

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 3 E3 ubiquitin-protein ligase RBX1 × 1 (P62877) Glomulin × 1 (Q92990) ZINC ION × 3 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 3 E3 ubiquitin-protein ligase RBX1 × 1 (P62877) Glomulin × 1 (Q92990) ZINC ION × 3 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 1
Chains and sequence ranges Author chain A; PDBConstruct 3–282; UniProt 411–690 Author chain C; PDBConstruct 3–282; UniProt 411–690

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 3 Cullin-1 × 1 (Q13616) Glomulin × 1 (Q92990) ZINC ION × 3 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 3 Cullin-1 × 1 (Q13616) Glomulin × 1 (Q92990) ZINC ION × 3 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 2
Chains and sequence ranges Author chain B; PDBConstruct 3–106; UniProt 5–108 Author chain D; PDBConstruct 3–106; UniProt 5–108

Glomulin

Homo sapiens

UniProt Q92990

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 Cullin-1 × 1 (Q13616) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZINC ION × 3 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 3 Cullin-1 × 1 (Q13616) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZINC ION × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name GLMN_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 3–596; UniProt 1–594 Author chain F; PDBConstruct 3–596; UniProt 1–594

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id4f52
Deposition date deposition_date2012-05-11
Structure title titleStructure of a Glomulin-RBX1-CUL1 complex
Keywords keywordsCullin-RING E3 Ligase, Inhibitor, Cell Cycle-Ligase-Signaling Protein complex; Cell Cycle/Ligase/Signaling Protein
Experimental Method methodX-RAY DIFFRACTION
▼

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.

4f52__assembly_1__model_1

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

Download this curve (.dat)

4f52__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.

4f52__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)35.66 Å
Rg (electron density)35.23 Å
Total Rg35.74 Å
Atom count7000
Residues865
Excluded volume126550 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 4f52__assembly_1__model_1 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 4f52__assembly_2__model_1 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

▼

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4f52b_
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.1 — RING finger domain, C3HC4
Domain ID domain_idd4f52d_
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.1 — RING finger domain, C3HC4

CATH v4.4 (6 domains)

Domain ID domain_id4f52A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id4f52A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily130 — Cullin; Chain C, Domain 2
Domain ID domain_id4f52B00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id4f52C01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id4f52C02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily130 — Cullin; Chain C, Domain 2
Domain ID domain_id4f52D00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
▶

7. Citations (1)