8rmf

Structure of the core ISC complex under turnover conditions (FDX2-bound in proximal conformation)

Method: ELECTRON MICROSCOPY Dmax: 135.9 Å Quality: GOOD

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

Isoform Mitochondrial of Cysteine desulfurase

Homo sapiens

UniProt Q9Y697

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 56–457 Chain E; UniProt 56–457 Non-standard monomer:Yes (specific site not provided by mmCIF) LYR motif-containing protein 4 × 2 (Q9HD34) Acyl carrier protein × 2 (P0A6A8) Isoform 1 of Iron-sulfur cluster assembly enzyme ISCU × 2 (Q9H1K1) Ferredoxin-2, mitochondrial × 1 (Q6P4F2) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 FE2 FE (II) ION × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.33 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.

19 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NFS1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–404; UniProt 56–457 Author chain E; PDBConstruct 3–404; UniProt 56–457

LYR motif-containing protein 4

Homo sapiens

UniProt Q9HD34

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 1–91 Chain F; UniProt 1–91 Not recorded Isoform Mitochondrial of Cysteine desulfurase × 2 (Q9Y697) Acyl carrier protein × 2 (P0A6A8) Isoform 1 of Iron-sulfur cluster assembly enzyme ISCU × 2 (Q9H1K1) Ferredoxin-2, mitochondrial × 1 (Q6P4F2) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 FE2 FE (II) ION × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.33 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.

19 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYRM4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 25–115; UniProt 1–91 Author chain F; PDBConstruct 25–115; UniProt 1–91

Acyl carrier protein

OrganismNot specified

UniProt P0A6A8

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 1–78 Chain G; UniProt 1–78 Not recorded Isoform Mitochondrial of Cysteine desulfurase × 2 (Q9Y697) LYR motif-containing protein 4 × 2 (Q9HD34) Isoform 1 of Iron-sulfur cluster assembly enzyme ISCU × 2 (Q9H1K1) Ferredoxin-2, mitochondrial × 1 (Q6P4F2) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 FE2 FE (II) ION × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.33 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.

39 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACP_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–78; UniProt 1–78 Author chain G; PDBConstruct 1–78; UniProt 1–78

Isoform 1 of Iron-sulfur cluster assembly enzyme ISCU

Homo sapiens

UniProt Q9H1K1

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 35–167 Chain H; UniProt 35–167 Not recorded Isoform Mitochondrial of Cysteine desulfurase × 2 (Q9Y697) LYR motif-containing protein 4 × 2 (Q9HD34) Acyl carrier protein × 2 (P0A6A8) Ferredoxin-2, mitochondrial × 1 (Q6P4F2) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 FE2 FE (II) ION × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.33 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ISCU_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 3–135; UniProt 35–167 Author chain H; PDBConstruct 3–135; UniProt 35–167

Ferredoxin-2, mitochondrial

Homo sapiens

UniProt Q6P4F2

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain I; UniProt 68–186 Not recorded Isoform Mitochondrial of Cysteine desulfurase × 2 (Q9Y697) LYR motif-containing protein 4 × 2 (Q9HD34) Acyl carrier protein × 2 (P0A6A8) Isoform 1 of Iron-sulfur cluster assembly enzyme ISCU × 2 (Q9H1K1) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 FE2 FE (II) ION × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.33 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.

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

View Construct and Data Evidence
UniProt name FDX2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 3–121; UniProt 68–186

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 8rmf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rmf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rmf
Deposition date deposition_date2024-01-05
最后修订 last_revision2024-12-18
Structure title titleStructure of the core ISC complex under turnover conditions (FDX2-bound in proximal conformation)
Keywords keywords;cysteine desulfurase, FeS biosynthesis, FeS biogenesis, mitochondria, Friedreich's ataxia, frataxin, ferredoxin, FDX2, iron-sulfur cluster, TRANSFERASE ;; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.80
Radius of gyration Rg (electron density) rg_electron37.54
Forward intensity I(0) i0419061000.00
Molecular weight molecular_weight164370.0 kDa
Excluded volume excluded_volume205140 ų
Envelope volume envelope_volume261830 ų
Hydration-shell volume shell_volume58217 ų
Envelope diameter envelope_diameter145.8
Shell Rg shell_rg43.56
Envelope Rg envelope_rg37.70
Shape Rg shape_rg37.54
Total Rg total_rg37.88
Total atoms total_atoms11508
Residues n_residues1462
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 dmax135.9
Rg (real space) rg_real37.76
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real4.1910e+08
I(0) uncertainty (real space) i0_real_error7.7850e+06
Rg (reciprocal space) rg_reciprocal37.79
I(0) (reciprocal space) i0_reciprocal419100000.0000
Solution quality estimate total_estimate0.8618
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.3
Skewness Skewness skewness0.328
Kurtosis Kurtosis kurtosis-0.223
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86060000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)