6wi2

Structure of human mitochondrial complex Nfs1-ISCU2-ISD11 with E.coli ACP1 at 1.95 A resolution (NIAU)2. N-terminal mutation of ISCU2 (L35) traps Nfs1 Cys loop in the active site of ISCU2 without metal present.

Method: X-RAY DIFFRACTION Dmax: 97.3 Å Quality: EXCELLENT

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 56–457 Not recorded LYR motif-containing protein 4 × 1 (Q9HD34) Acyl carrier protein × 1 (B7MJ81) Iron-sulfur cluster assembly enzyme ISCU, mitochondrial × 1 (Q9H1K1) PLP PYRIDOXAL-5'-PHOSPHATE × 1 EDO 1,2-ETHANEDIOL × 36 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 10 PG4 TETRAETHYLENE GLYCOL × 2 ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 PGE TRIETHYLENE GLYCOL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;288 K;0.1 M MES pH 5.5 22.5 % PEG 400 Resolution 1.95 Å R-free 0.185

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 5–406; 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–91 Not recorded Cysteine desulfurase, mitochondrial × 1 (Q9Y697) Acyl carrier protein × 1 (B7MJ81) Iron-sulfur cluster assembly enzyme ISCU, mitochondrial × 1 (Q9H1K1) PLP PYRIDOXAL-5'-PHOSPHATE × 1 EDO 1,2-ETHANEDIOL × 36 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 10 PG4 TETRAETHYLENE GLYCOL × 2 ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 PGE TRIETHYLENE GLYCOL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;288 K;0.1 M MES pH 5.5 22.5 % PEG 400 Resolution 1.95 Å R-free 0.185

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 1–91; UniProt 1–91

Acyl carrier protein

OrganismNot specified

UniProt B7MJ81

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 2–78 Not recorded Cysteine desulfurase, mitochondrial × 1 (Q9Y697) LYR motif-containing protein 4 × 1 (Q9HD34) Iron-sulfur cluster assembly enzyme ISCU, mitochondrial × 1 (Q9H1K1) PLP PYRIDOXAL-5'-PHOSPHATE × 1 EDO 1,2-ETHANEDIOL × 36 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 10 PG4 TETRAETHYLENE GLYCOL × 2 ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 PGE TRIETHYLENE GLYCOL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;288 K;0.1 M MES pH 5.5 22.5 % PEG 400 Resolution 1.95 Å R-free 0.185

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.

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

View Construct and Data Evidence
UniProt name ACP_ECO45
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–77; UniProt 2–78

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 10–142 Not recorded Cysteine desulfurase, mitochondrial × 1 (Q9Y697) LYR motif-containing protein 4 × 1 (Q9HD34) Acyl carrier protein × 1 (B7MJ81) PLP PYRIDOXAL-5'-PHOSPHATE × 1 EDO 1,2-ETHANEDIOL × 36 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 10 PG4 TETRAETHYLENE GLYCOL × 2 ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 PGE TRIETHYLENE GLYCOL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;288 K;0.1 M MES pH 5.5 22.5 % PEG 400 Resolution 1.95 Å R-free 0.185

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 Q9H1K1-2
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 3–135; UniProt 10–142

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 6wi2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wi2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wi2
Deposition date deposition_date2020-04-08
Structure title titleStructure of human mitochondrial complex Nfs1-ISCU2-ISD11 with E.coli ACP1 at 1.95 A resolution (NIAU)2. N-terminal mutation of ISCU2 (L35) traps Nfs1 Cys loop in the active site of ISCU2 without metal present.
Keywords keywordscomplex, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.90
Radius of gyration Rg (electron density) rg_electron30.22
Forward intensity I(0) i0104031000.00
Molecular weight molecular_weight80187.0 kDa
Excluded volume excluded_volume100360 ų
Envelope volume envelope_volume125210 ų
Hydration-shell volume shell_volume35349 ų
Envelope diameter envelope_diameter106.8
Shell Rg shell_rg36.67
Envelope Rg envelope_rg30.44
Shape Rg shape_rg30.26
Total Rg total_rg30.68
Total atoms total_atoms5602
Residues n_residues686
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 dmax97.3
Rg (real space) rg_real30.90
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.0400e+08
I(0) uncertainty (real space) i0_real_error1.5480e+06
Rg (reciprocal space) rg_reciprocal30.90
I(0) (reciprocal space) i0_reciprocal104000000.0000
Solution quality estimate total_estimate0.9015
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.276
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30330000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.884

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd6wi2a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.67 — PLP-dependent transferase-like
Superfamily Superfamily superfamilyc.67.1 — PLP-dependent transferases
Family Family familyc.67.1.3 — Cystathionine synthase-like
Domain ID domain_idd6wi2a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6wi2b_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.71 — LYR proteins from mammalian respiratory complex I
Superfamily Superfamily superfamilyf.71.1 — LYR protein-like
Family Family familyf.71.1.1 — LYR proteins
Domain ID domain_idd6wi2c_
Class classa — All alpha proteins
Fold Fold folda.28 — Acyl carrier protein-like
Superfamily Superfamily superfamilya.28.1 — ACP-like
Family Family familya.28.1.1 — Acyl-carrier protein (ACP)
Domain ID domain_idd6wi2d1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.224 — SufE/NifU
Superfamily Superfamily superfamilyd.224.1 — SufE/NifU
Family Family familyd.224.1.2 — NifU/IscU domain
Domain ID domain_idd6wi2d2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id6wi2A02
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_id6wi2D01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1010 — Sufe protein. Chain: A
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)