5wgb

Crystal Structure of the Human mitochondrial Cysteine Desulfurase in complex with ISD11 and E. coli ACP1 protein at 2.75A

Method: X-RAY DIFFRACTION Dmax: 90.8 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 56–457 Not recorded LYR motif-containing protein 4 × 1 (Q9HD34) Acyl carrier protein × 1 (B7MJ81) PLP PYRIDOXAL-5'-PHOSPHATE × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;285 K;0.1 M MES pH 6.5 0.3 M Ammonium Acetate 20 mM Calcium Acetate 20 mM CaCl2 19 % isopropanol Resolution 2.75 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 25–426; 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–91 Not recorded Cysteine desulfurase, mitochondrial × 1 (Q9Y697) Acyl carrier protein × 1 (B7MJ81) PLP PYRIDOXAL-5'-PHOSPHATE × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;285 K;0.1 M MES pH 6.5 0.3 M Ammonium Acetate 20 mM Calcium Acetate 20 mM CaCl2 19 % isopropanol Resolution 2.75 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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 2–78 Not recorded Cysteine desulfurase, mitochondrial × 1 (Q9Y697) LYR motif-containing protein 4 × 1 (Q9HD34) PLP PYRIDOXAL-5'-PHOSPHATE × 1 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;285 K;0.1 M MES pH 6.5 0.3 M Ammonium Acetate 20 mM Calcium Acetate 20 mM CaCl2 19 % isopropanol Resolution 2.75 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

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 5wgb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wgb
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5wgb
Deposition date deposition_date2017-07-13
Structure title titleCrystal Structure of the Human mitochondrial Cysteine Desulfurase in complex with ISD11 and E. coli ACP1 protein at 2.75A
Keywords keywordsHuman mitochondrial cysteine desulfurse LYR Motif containing protein 4 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_guinier26.50
Radius of gyration Rg (electron density) rg_electron25.87
Forward intensity I(0) i036434100.00
Molecular weight molecular_weight46191.0 kDa
Excluded volume excluded_volume57676 ų
Envelope volume envelope_volume74750 ų
Hydration-shell volume shell_volume25178 ų
Envelope diameter envelope_diameter93.2
Shell Rg shell_rg31.73
Envelope Rg envelope_rg26.15
Shape Rg shape_rg25.91
Total Rg total_rg26.40
Total atoms total_atoms3247
Residues n_residues437
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 dmax90.8
Rg (real space) rg_real26.64
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real3.6430e+07
I(0) uncertainty (real space) i0_real_error5.5070e+05
Rg (reciprocal space) rg_reciprocal26.60
I(0) (reciprocal space) i0_reciprocal36430000.0000
Solution quality estimate total_estimate0.8603
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis-0.128
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7532000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.868; Smooth: 0.857

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5wgbb_
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_idd5wgbc_
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)

CATH v4.4 (1 domains)

Domain ID domain_id5wgbA02
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)

8. Citations (1)

9. Files and Curves (10)