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Architecture of mammalian fatty acid synthase

Analyse Architecture of mammalian fatty acid synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2CF2
Type
protein
Length
3,146 residues
Chains
10
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fatty acid synthase, ks domain; Fatty acid synthase, mat domain; Fatty acid synthase, dh…
EC
2.3.1.85
Pockets
20 · best druggability 0.69

Structure

x-ray diffraction · 5 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, JFatty acid synthase, ks domain (EC 2.3.1.85)protein4060% helix, 0% strand—
B, KFatty acid synthase, mat domain (EC 2.3.1.85)protein3040% helix, 0% strand—
C, LFatty acid synthase, dh domain (EC 2.3.1.85)protein3420% helix, 0% strand—
D, MFatty acid synthase, er domain (EC 2.3.1.85)protein2950% helix, 0% strand—
E, NFatty acid synthase, kr domain (EC 2.3.1.85)protein2260% helix, 0% strand—

Pockets

20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15410.690.77120empty
26250.660.74117empty
35560.640.73108empty
44960.620.7397empty
52140.500.7357empty

Interfaces

13 interfaces between chains.

  • C–L · 625 Ų buried · 0 hydrogen bonds · protein-protein
  • A–J · 488 Ų buried · 0 hydrogen bonds · protein-protein
  • J–L · 361 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 288 Ų buried · 0 hydrogen bonds · protein-protein
  • A–L · 247 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2CF2 · Architecture of mammalian fatty acid synthase · the same entry in another collection · chain A against A, TM-score 1.00

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