2was

Structure of the fungal type I FAS PPT domain

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE

SACCHAROMYCES CEREVISIAE

UniProt P19097

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 3 water × 3 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 3 water × 3 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 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–122; UniProt 1766–1887 Author chain D; PDBConstruct 1–122; UniProt 1766–1887 Author chain E; PDBConstruct 1–122; UniProt 1766–1887 Author chain B; PDBConstruct 1–122; UniProt 1766–1887 Author chain C; PDBConstruct 1–122; UniProt 1766–1887 Author chain F; PDBConstruct 1–122; UniProt 1766–1887

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id2was
Deposition date deposition_date2009-02-15
Structure title titleStructure of the fungal type I FAS PPT domain
Keywords keywords;COA, FAS, PPT, NAD, NADP, TRANSFERASE, PHOSPHOPROTEIN, OXIDOREDUCTASE, LIPID SYNTHESIS, PHOSPHOPANTETHEINE TRANSFERASE, PHOSPHOPANTETHEINE, MULTIFUNCTIONAL ENZYME, FATTY ACID BIOSYNTHESIS, PHOSPHOPANTETHEINYLATION ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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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.

2was__assembly_1__model_1

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

Download this curve (.dat)

2was__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2was__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)21.05 Å
Rg (electron density)19.87 Å
Total Rg20.73 Å
Atom count2535
Residues342
Excluded volume44934 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2was__assembly_1__model_1 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 2was__assembly_2__model_1 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2wasa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.150 — 4'-phosphopantetheinyl transferase
Superfamily Superfamily superfamilyd.150.1 — 4'-phosphopantetheinyl transferase
Family Family familyd.150.1.0 — automated matches
Domain ID domain_idd2wasb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.150 — 4'-phosphopantetheinyl transferase
Superfamily Superfamily superfamilyd.150.1 — 4'-phosphopantetheinyl transferase
Family Family familyd.150.1.0 — automated matches
Domain ID domain_idd2wasc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.150 — 4'-phosphopantetheinyl transferase
Superfamily Superfamily superfamilyd.150.1 — 4'-phosphopantetheinyl transferase
Family Family familyd.150.1.0 — automated matches
Domain ID domain_idd2wasd_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.150 — 4'-phosphopantetheinyl transferase
Superfamily Superfamily superfamilyd.150.1 — 4'-phosphopantetheinyl transferase
Family Family familyd.150.1.0 — automated matches
Domain ID domain_idd2wase_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.150 — 4'-phosphopantetheinyl transferase
Superfamily Superfamily superfamilyd.150.1 — 4'-phosphopantetheinyl transferase
Family Family familyd.150.1.0 — automated matches
Domain ID domain_idd2wasf_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.150 — 4'-phosphopantetheinyl transferase
Superfamily Superfamily superfamilyd.150.1 — 4'-phosphopantetheinyl transferase
Family Family familyd.150.1.0 — automated matches

CATH v4.4 (6 domains)

Domain ID domain_id2wasA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily20 — 4'-phosphopantetheinyl transferase domain
Domain ID domain_id2wasB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily20 — 4'-phosphopantetheinyl transferase domain
Domain ID domain_id2wasC00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily20 — 4'-phosphopantetheinyl transferase domain
Domain ID domain_id2wasD00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily20 — 4'-phosphopantetheinyl transferase domain
Domain ID domain_id2wasE00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily20 — 4'-phosphopantetheinyl transferase domain
Domain ID domain_id2wasF00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily20 — 4'-phosphopantetheinyl transferase domain
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7. Citations (1)