5wlw

Crystal Structure of the Human Mitochondrial Cysteine Desulfurase with active Cysteine Loop within ISCU1 active site, coordinating Zn ion. Complexed with human ISD11 and E. coli ACP1 at 3.3A.

Method: X-RAY DIFFRACTION Dmax: 137.3 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 × 8 PDB declaration: octameric(8) 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 (B7MJ81) 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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;285 K;0.1 M MES pH 7.0 15 % PEG 3350 Resolution 3.32 Å R-free 0.255

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 Author chain E; 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 × 8 PDB declaration: octameric(8) 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 (B7MJ81) 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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;285 K;0.1 M MES pH 7.0 15 % PEG 3350 Resolution 3.32 Å R-free 0.255

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 Author chain F; PDBConstruct 1–91; UniProt 1–91

Acyl carrier protein

Escherichia coli O45:K1 (strain S88 / ExPEC)

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 2–78 Chain G; UniProt 2–78 Not recorded Cysteine desulfurase, mitochondrial × 2 (Q9Y697) LYR motif-containing protein 4 × 2 (Q9HD34) 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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;285 K;0.1 M MES pH 7.0 15 % PEG 3350 Resolution 3.32 Å R-free 0.255

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 Author chain G; 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 1–142 Chain H; UniProt 1–142 Not recorded Cysteine desulfurase, mitochondrial × 2 (Q9Y697) LYR motif-containing protein 4 × 2 (Q9HD34) Acyl carrier protein × 2 (B7MJ81) 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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;285 K;0.1 M MES pH 7.0 15 % PEG 3350 Resolution 3.32 Å R-free 0.255

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 1–142; UniProt 1–142 Author chain H; PDBConstruct 1–142; UniProt 1–142

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 5wlw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wlw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5wlw
Deposition date deposition_date2017-07-27
Structure title titleCrystal Structure of the Human Mitochondrial Cysteine Desulfurase with active Cysteine Loop within ISCU1 active site, coordinating Zn ion. Complexed with human ISD11 and E. coli ACP1 at 3.3A.
Keywords keywords;Human mitochondrial cysteine desulfurse LYR Motif containing protein 4 Iron-Sulfur Cluster Scaffold Protein ISCU1 with Zn in the active site Acyl Carrier Protein 1 (E.coli), TRANSFERASE ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.86
Radius of gyration Rg (electron density) rg_electron36.47
Forward intensity I(0) i0308168000.00
Molecular weight molecular_weight140480.0 kDa
Excluded volume excluded_volume175110 ų
Envelope volume envelope_volume226590 ų
Hydration-shell volume shell_volume52478 ų
Envelope diameter envelope_diameter147.2
Shell Rg shell_rg41.98
Envelope Rg envelope_rg36.94
Shape Rg shape_rg36.51
Total Rg total_rg36.69
Total atoms total_atoms9866
Residues n_residues1357
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 dmax137.3
Rg (real space) rg_real36.89
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real3.0820e+08
I(0) uncertainty (real space) i0_real_error5.6360e+06
Rg (reciprocal space) rg_reciprocal36.87
I(0) (reciprocal space) i0_reciprocal308200000.0000
Solution quality estimate total_estimate0.8332
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.9
Skewness Skewness skewness0.405
Kurtosis Kurtosis kurtosis-0.012
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77450000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.660; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.885; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5wlwA02
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_id5wlwD01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1010 — Sufe protein. Chain: A
Homologous superfamily homologous superfamily10
Domain ID domain_id5wlwE02
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_id5wlwH01
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)