6nzu

Structure of the human frataxin-bound iron-sulfur cluster assembly complex

Method: ELECTRON MICROSCOPY Dmax: 141.4 Å Quality: GOOD

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

Cysteine desulfurase, mitochondrial

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 56–457 Chain E; UniProt 56–457 Fragment:UNP residues 56-457 LYR motif-containing protein 4 × 2 (Q9HD34) Acyl carrier protein × 2 (A0A437HBF4) Iron-sulfur cluster assembly enzyme ISCU, mitochondrial × 2 (Q9H1K1) Frataxin, mitochondrial × 2 (Q16595) PLP PYRIDOXAL-5'-PHOSPHATE × 2 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 2–403; UniProt 56–457 Author chain E; PDBConstruct 2–403; 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain B; UniProt 1–91 Chain F; UniProt 1–91 Not recorded Cysteine desulfurase, mitochondrial × 2 (Q9Y697) Acyl carrier protein × 2 (A0A437HBF4) Iron-sulfur cluster assembly enzyme ISCU, mitochondrial × 2 (Q9H1K1) Frataxin, mitochondrial × 2 (Q16595) PLP PYRIDOXAL-5'-PHOSPHATE × 2 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 2–92; UniProt 1–91 Author chain F; PDBConstruct 2–92; UniProt 1–91

Acyl carrier protein

Escherichia coli

UniProt A0A437HBF4

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 1–74 Chain G; UniProt 1–74 Not recorded Cysteine desulfurase, mitochondrial × 2 (Q9Y697) LYR motif-containing protein 4 × 2 (Q9HD34) Iron-sulfur cluster assembly enzyme ISCU, mitochondrial × 2 (Q9H1K1) Frataxin, mitochondrial × 2 (Q16595) PLP PYRIDOXAL-5'-PHOSPHATE × 2 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 A0A437HBF4_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–74; UniProt 1–74 Author chain G; PDBConstruct 1–74; UniProt 1–74

Iron-sulfur cluster assembly enzyme ISCU, mitochondrial

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 35–157 Chain H; UniProt 35–157 Fragment:UNP residues 35-157 Cysteine desulfurase, mitochondrial × 2 (Q9Y697) LYR motif-containing protein 4 × 2 (Q9HD34) Acyl carrier protein × 2 (A0A437HBF4) Frataxin, mitochondrial × 2 (Q16595) PLP PYRIDOXAL-5'-PHOSPHATE × 2 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 2–124; UniProt 35–157 Author chain H; PDBConstruct 2–124; UniProt 35–157

Frataxin, mitochondrial

Homo sapiens

UniProt Q16595

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain I; UniProt 81–210 Chain J; UniProt 81–210 Fragment:UNP residues 81-210 Cysteine desulfurase, mitochondrial × 2 (Q9Y697) LYR motif-containing protein 4 × 2 (Q9HD34) Acyl carrier protein × 2 (A0A437HBF4) Iron-sulfur cluster assembly enzyme ISCU, mitochondrial × 2 (Q9H1K1) PLP PYRIDOXAL-5'-PHOSPHATE × 2 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

18 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FRDA_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 3–132; UniProt 81–210 Author chain J; PDBConstruct 3–132; UniProt 81–210

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 6nzu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6nzu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6nzu
Deposition date deposition_date2019-02-14
Structure title titleStructure of the human frataxin-bound iron-sulfur cluster assembly complex
Keywords keywordshuman frataxin-bound iron-sulfur cluster assembly complex, TRANSFERASE, OXIDOREDUCTASE; TRANSFERASE, OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.84
Radius of gyration Rg (electron density) rg_electron38.56
Forward intensity I(0) i0484015000.00
Molecular weight molecular_weight178520.0 kDa
Excluded volume excluded_volume223380 ų
Envelope volume envelope_volume295090 ų
Hydration-shell volume shell_volume63329 ų
Envelope diameter envelope_diameter150.3
Shell Rg shell_rg44.88
Envelope Rg envelope_rg38.60
Shape Rg shape_rg38.55
Total Rg total_rg38.93
Total atoms total_atoms12528
Residues n_residues1588
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 dmax141.4
Rg (real space) rg_real38.79
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real4.8400e+08
I(0) uncertainty (real space) i0_real_error9.5320e+06
Rg (reciprocal space) rg_reciprocal38.82
I(0) (reciprocal space) i0_reciprocal484000000.0000
Solution quality estimate total_estimate0.8528
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.3
Skewness Skewness skewness0.336
Kurtosis Kurtosis kurtosis-0.206
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha129000000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.704; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id6nzuA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Domain ID domain_id6nzuD01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1010 — Sufe protein. Chain: A
Homologous superfamily homologous superfamily10
Domain ID domain_id6nzuE02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Domain ID domain_id6nzuH01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1010 — Sufe protein. Chain: A
Homologous superfamily homologous superfamily10
Domain ID domain_id6nzuI00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology920 — Metal Transport, Frataxin; Chain A
Homologous superfamily homologous superfamily10 — Frataxin/CyaY
Domain ID domain_id6nzuJ00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology920 — Metal Transport, Frataxin; Chain A
Homologous superfamily homologous superfamily10 — Frataxin/CyaY

8. Citations (1)

9. Files and Curves (10)