8tvt

Structure of human Cysteine desulfurase Nfs1 with L-propargylglycine bound to active site PLP in complex with ISD11, Acp1 and ISCU2

Method: X-RAY DIFFRACTION Dmax: 100.6 Å Quality: GOOD

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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 56–454 Not recorded LYR motif-containing protein 4 × 1 (Q9HD34) Acyl carrier protein × 1 (A7ZKJ7) Iron-sulfur cluster assembly enzyme ISCU × 1 (Q9H1K1) EDO 1,2-ETHANEDIOL × 30 PLP PYRIDOXAL-5'-PHOSPHATE × 1 LPH L-Propargylglycine × 1 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 8 PG4 TETRAETHYLENE GLYCOL × 2 P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL × 1 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 PGE TRIETHYLENE GLYCOL × 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 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;288 K;0.1 M MES pH 6.5 22.5 % PEG 400 Resolution 2.00 Å R-free 0.186

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 5–403; UniProt 56–454

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 × 1 (Q9Y697) Acyl carrier protein × 1 (A7ZKJ7) Iron-sulfur cluster assembly enzyme ISCU × 1 (Q9H1K1) EDO 1,2-ETHANEDIOL × 30 PLP PYRIDOXAL-5'-PHOSPHATE × 1 LPH L-Propargylglycine × 1 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 8 PG4 TETRAETHYLENE GLYCOL × 2 P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL × 1 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 PGE TRIETHYLENE GLYCOL × 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 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;288 K;0.1 M MES pH 6.5 22.5 % PEG 400 Resolution 2.00 Å R-free 0.186

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

Escherichia coli

UniProt A7ZKJ7

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 2–77 Not recorded Cysteine desulfurase × 1 (Q9Y697) LYR motif-containing protein 4 × 1 (Q9HD34) Iron-sulfur cluster assembly enzyme ISCU × 1 (Q9H1K1) EDO 1,2-ETHANEDIOL × 30 PLP PYRIDOXAL-5'-PHOSPHATE × 1 LPH L-Propargylglycine × 1 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 8 PG4 TETRAETHYLENE GLYCOL × 2 P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL × 1 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 PGE TRIETHYLENE GLYCOL × 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 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;288 K;0.1 M MES pH 6.5 22.5 % PEG 400 Resolution 2.00 Å R-free 0.186

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 ACP_ECO24
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–76; UniProt 2–77

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 35–167 Not recorded Cysteine desulfurase × 1 (Q9Y697) LYR motif-containing protein 4 × 1 (Q9HD34) Acyl carrier protein × 1 (A7ZKJ7) EDO 1,2-ETHANEDIOL × 30 PLP PYRIDOXAL-5'-PHOSPHATE × 1 LPH L-Propargylglycine × 1 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 8 PG4 TETRAETHYLENE GLYCOL × 2 P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL × 1 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 PGE TRIETHYLENE GLYCOL × 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 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;288 K;0.1 M MES pH 6.5 22.5 % PEG 400 Resolution 2.00 Å R-free 0.186

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

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 8tvt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tvt
Deposition date deposition_date2023-08-18
Structure title titleStructure of human Cysteine desulfurase Nfs1 with L-propargylglycine bound to active site PLP in complex with ISD11, Acp1 and ISCU2
Keywords keywordsNfs1, PG-PLP bound, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.74
Radius of gyration Rg (electron density) rg_electron30.15
Forward intensity I(0) i0101240000.00
Molecular weight molecular_weight79452.0 kDa
Excluded volume excluded_volume99584 ų
Envelope volume envelope_volume122820 ų
Hydration-shell volume shell_volume34873 ų
Envelope diameter envelope_diameter109.6
Shell Rg shell_rg36.44
Envelope Rg envelope_rg30.43
Shape Rg shape_rg30.18
Total Rg total_rg30.61
Total atoms total_atoms5552
Residues n_residues684
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 dmax100.6
Rg (real space) rg_real30.75
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real1.0120e+08
I(0) uncertainty (real space) i0_real_error1.7350e+06
Rg (reciprocal space) rg_reciprocal30.75
I(0) (reciprocal space) i0_reciprocal101200000.0000
Solution quality estimate total_estimate0.8982
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.0
Skewness Skewness skewness0.290
Kurtosis Kurtosis kurtosis-0.559
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27580000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

8. Citations (1)

9. Files and Curves (10)