6odd

Crystal structure of the human complex ACP-ISD11

Method: X-RAY DIFFRACTION Dmax: 58.5 Å Quality: GOOD

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

Acyl carrier protein, mitochondrial

Homo sapiens

UniProt O14561

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 72–156 Not recorded LYR motif-containing protein 4 × 2 (Q9HD34) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;The drop was a 1:1 mix of protein (in 10 mM Tris buffer, 25 mM NaCl, pH 7.5) and reservoir solution (0.1 M Tris pH 9.1, 0.1 M CaCl2, 23% tert-butanol) Resolution 2.00 Å R-free 0.216
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 72–156 Not recorded LYR motif-containing protein 4 × 1 (Q9HD34) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;The drop was a 1:1 mix of protein (in 10 mM Tris buffer, 25 mM NaCl, pH 7.5) and reservoir solution (0.1 M Tris pH 9.1, 0.1 M CaCl2, 23% tert-butanol) Resolution 2.00 Å R-free 0.216

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.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACPM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–85; UniProt 72–156

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 5–78 Not recorded Acyl carrier protein, mitochondrial × 2 (O14561) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;The drop was a 1:1 mix of protein (in 10 mM Tris buffer, 25 mM NaCl, pH 7.5) and reservoir solution (0.1 M Tris pH 9.1, 0.1 M CaCl2, 23% tert-butanol) Resolution 2.00 Å R-free 0.216
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 5–78 Not recorded Acyl carrier protein, mitochondrial × 1 (O14561) 8Q1 S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;The drop was a 1:1 mix of protein (in 10 mM Tris buffer, 25 mM NaCl, pH 7.5) and reservoir solution (0.1 M Tris pH 9.1, 0.1 M CaCl2, 23% tert-butanol) Resolution 2.00 Å R-free 0.216

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 LYRM4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–74; UniProt 5–78

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 6odd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6odd
Deposition date deposition_date2019-03-26
Structure title titleCrystal structure of the human complex ACP-ISD11
Keywords keywordsIron Sulfur Clusters, Cysteine desulfurase activity regulator, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.15
Radius of gyration Rg (electron density) rg_electron17.28
Forward intensity I(0) i06698180.00
Molecular weight molecular_weight19196.0 kDa
Excluded volume excluded_volume24215 ų
Envelope volume envelope_volume28701 ų
Hydration-shell volume shell_volume14527 ų
Envelope diameter envelope_diameter60.2
Shell Rg shell_rg22.63
Envelope Rg envelope_rg17.55
Shape Rg shape_rg17.30
Total Rg total_rg18.16
Total atoms total_atoms2714
Residues n_residues159
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 dmax58.5
Rg (real space) rg_real18.11
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real6.6980e+06
I(0) uncertainty (real space) i0_real_error7.5750e+04
Rg (reciprocal space) rg_reciprocal18.11
I(0) (reciprocal space) i0_reciprocal6698000.0000
Solution quality estimate total_estimate0.8156
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.413
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1568000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6odda_
Class classa — All alpha proteins
Fold Fold folda.28 — Acyl carrier protein-like
Superfamily Superfamily superfamilya.28.1 — ACP-like
Family Family familya.28.1.0 — automated matches
Domain ID domain_idd6oddb_
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

8. Citations (1)

9. Files and Curves (10)