6vcd

Cryo-EM structure of IRP2-FBXL5-SKP1 complex

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

Iron-responsive element binding protein 2, isoform CRA_a

Homo sapiens

UniProt D3DW85

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 F-box/LRR-repeat protein 5 × 1 (Q9UKA1) S-phase kinase-associated protein 1 × 1 (P63208) FE2/S2 (INORGANIC) CLUSTER × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name D3DW85_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–963; UniProt 1–963

F-box/LRR-repeat protein 5

Homo sapiens

UniProt Q9UKA1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 Iron-responsive element binding protein 2, isoform CRA_a × 1 (D3DW85) S-phase kinase-associated protein 1 × 1 (P63208) FE2/S2 (INORGANIC) CLUSTER × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FBXL5_HUMAN
Isoform Q9UKA1-2
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–492; UniProt 183–674

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 3 Iron-responsive element binding protein 2, isoform CRA_a × 1 (D3DW85) F-box/LRR-repeat protein 5 × 1 (Q9UKA1) FE2/S2 (INORGANIC) CLUSTER × 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

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_id6vcd
Deposition date deposition_date2019-12-20
Structure title titleCryo-EM structure of IRP2-FBXL5-SKP1 complex
Keywords keywordsE3 ligase, [2Fe-2S] cluster, Iron metabolism, 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.

6vcd__assembly_1__model_1

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

Download this curve (.dat)

6vcd__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.

6vcd__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)36.38 Å
Rg (electron density)36.20 Å
Total Rg36.61 Å
Atom count8082
Residues1033
Excluded volume144880 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6vcd__assembly_1__model_1 trimeric (3) 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 (4)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6vcdc1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.0 — automated matches
Domain ID domain_idd6vcdc2
Class classa — All alpha proteins
Fold Fold folda.157 — Skp1 dimerisation domain-like
Superfamily Superfamily superfamilya.157.1 — Skp1 dimerisation domain-like
Family Family familya.157.1.1 — Skp1 dimerisation domain-like
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7. Citations (1)