9n50

Crosslinked Crystal Structure of Human Mitochondrial Ketosynthase, OXSM, and Crosslinker-crypto Human Mitochondrial Acyl Carrier Protein, C8aBr-mACP

Method: X-RAY DIFFRACTION Dmax: 93.9 Å Quality: GOOD

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

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial

Homo sapiens

UniProt Q9NWU1

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 38–459 Chain B; UniProt 38–459 Fragment:residues 38-459 Acyl carrier protein, mitochondrial × 1 (O14561) A1BMZ N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-octanamidoethyl)-beta-alaninamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.5 M ammonium sulfate, 1 M lithium sulfate, and 0.1 M sodium citrate pH 5.6 Resolution 2.50 Å

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OXSM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–425; UniProt 38–459 Author chain B; PDBConstruct 4–425; UniProt 38–459

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 69–156 Not recorded 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial × 2 (Q9NWU1) A1BMZ N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-octanamidoethyl)-beta-alaninamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.5 M ammonium sulfate, 1 M lithium sulfate, and 0.1 M sodium citrate pH 5.6 Resolution 2.50 Å

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 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACPM_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–88; UniProt 69–156

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 9n50

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n50
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n50
Deposition date deposition_date2025-02-03
最后修订 last_revision2025-09-24
Structure title titleCrosslinked Crystal Structure of Human Mitochondrial Ketosynthase, OXSM, and Crosslinker-crypto Human Mitochondrial Acyl Carrier Protein, C8aBr-mACP
Keywords keywordsCrosslinked Complex, Human mitochondria, Type II Fatty Acid Biosynthesis, Ketosynthase, 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_guinier27.89
Radius of gyration Rg (electron density) rg_electron27.19
Forward intensity I(0) i0299565000.00
Molecular weight molecular_weight91742.0 kDa
Excluded volume excluded_volume88354 ų
Envelope volume envelope_volume143180 ų
Hydration-shell volume shell_volume41873 ų
Envelope diameter envelope_diameter99.8
Shell Rg shell_rg36.07
Envelope Rg envelope_rg27.53
Shape Rg shape_rg27.21
Total Rg total_rg27.74
Total atoms total_atoms6934
Residues n_residues924
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 dmax93.9
Rg (real space) rg_real27.73
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real2.9960e+08
I(0) uncertainty (real space) i0_real_error4.1490e+06
Rg (reciprocal space) rg_reciprocal27.78
I(0) (reciprocal space) i0_reciprocal299600000.0000
Solution quality estimate total_estimate0.7970
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.228
Kurtosis Kurtosis kurtosis-0.346
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha65100000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.786; Stabil: 1.000; 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 (4)

8. Citations (1)

9. Files and Curves (10)