9d4a

Atomic model of Ketoacyl Reductase domain and 4 helical bundle of S. cerevisiae Fatty Acid Synthase (FAS) in complex with octanoyl-CoA (in vitro binding)

Method: ELECTRON MICROSCOPY
▼

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

Fatty acid synthase subunit beta

OrganismNot specified

UniProt P07149

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 12 Fatty acid synthase subunit alpha × 6 (P19097) FLAVIN MONONUCLEOTIDE × 6 S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] octanethioate × 6 water × 12 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FAS1_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–2051; UniProt 1–2051 Author chain E; PDBConstruct 1–2051; UniProt 1–2051 Author chain I; PDBConstruct 1–2051; UniProt 1–2051 Author chain M; PDBConstruct 1–2051; UniProt 1–2051 Author chain Q; PDBConstruct 1–2051; UniProt 1–2051 Author chain U; PDBConstruct 1–2051; UniProt 1–2051

Fatty acid synthase subunit alpha

OrganismNot specified

UniProt P19097

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 12 Fatty acid synthase subunit beta × 6 (P07149) FLAVIN MONONUCLEOTIDE × 6 S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] octanethioate × 6 water × 12 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FAS2_YEAST
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1887; UniProt 1–1887 Author chain F; PDBConstruct 1–1887; UniProt 1–1887 Author chain J; PDBConstruct 1–1887; UniProt 1–1887 Author chain N; PDBConstruct 1–1887; UniProt 1–1887 Author chain R; PDBConstruct 1–1887; UniProt 1–1887 Author chain V; PDBConstruct 1–1887; UniProt 1–1887

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id9d4a
Deposition date deposition_date2024-08-12
Structure title titleAtomic model of Ketoacyl Reductase domain and 4 helical bundle of S. cerevisiae Fatty Acid Synthase (FAS) in complex with octanoyl-CoA (in vitro binding)
Keywords keywordsoctanoyl-CoA, FAS, allosteric inhibition, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY
▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9d4a__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9d4a__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 1010 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9d4a__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)0.00 Å
Rg (electron density)102.10 Å
Total Rg102.10 Å
Atom count160398
Residues20604
Excluded volume2867100 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9d4a__assembly_1__model_1 dodecameric (12) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

▶

7. Citations (1)