6vcd

Cryo-EM structure of IRP2-FBXL5-SKP1 complex

Method: ELECTRON MICROSCOPY Dmax: 126.0 Å Quality: GOOD

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–963 Not recorded F-box/LRR-repeat protein 5 × 1 (Q9UKA1) S-phase kinase-associated protein 1 × 1 (P63208) FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

No other PDB entry for the same UniProt protein was found.

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 183–674 Fragment:UNP residues 183-674 Iron-responsive element binding protein 2, isoform CRA_a × 1 (D3DW85) S-phase kinase-associated protein 1 × 1 (P63208) FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

5 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–163 Not recorded Iron-responsive element binding protein 2, isoform CRA_a × 1 (D3DW85) F-box/LRR-repeat protein 5 × 1 (Q9UKA1) FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

71 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 6vcd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6vcd
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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

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

Radius of gyration Rg (Guinier) rg_guinier36.38
Radius of gyration Rg (electron density) rg_electron36.20
Forward intensity I(0) i0194529000.00
Molecular weight molecular_weight114890.0 kDa
Excluded volume excluded_volume144880 ų
Envelope volume envelope_volume193250 ų
Hydration-shell volume shell_volume45061 ų
Envelope diameter envelope_diameter133.8
Shell Rg shell_rg41.89
Envelope Rg envelope_rg35.99
Shape Rg shape_rg36.19
Total Rg total_rg36.61
Total atoms total_atoms8082
Residues n_residues1033
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 dmax126.0
Rg (real space) rg_real36.48
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real1.9450e+08
I(0) uncertainty (real space) i0_real_error3.1560e+06
Rg (reciprocal space) rg_reciprocal36.42
I(0) (reciprocal space) i0_reciprocal194500000.0000
Solution quality estimate total_estimate0.8614
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.9
Skewness Skewness skewness0.425
Kurtosis Kurtosis kurtosis-0.135
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37160000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.923; Smooth: 0.844

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. 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

8. Citations (1)

9. Files and Curves (10)