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Acyl carrier protein (acp) domain bound to dehydratase (dh) domain in fungal fatty acid synthase (fas)

Analyse Acyl carrier protein (acp) domain bound to dehydratase (dh) domain in fungal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WC7
Type
protein
Length
585 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fatty acid synthase subunit beta; Fatty acid synthase subunit alpha
EC
2.3.1.86, 4.2.1.59, 1.3.1.9, 2.3.1.38, 2.3.1.39, 3.1.2.14, 1.1.1.100, 2.3.1.41
UniProt
P07149, P19097
Pockets
6 · best druggability 0.80

Structure

electron microscopy · 2 distinct chains · 29% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
GFatty acid synthase subunit beta (EC 2.3.1.86, 4.2.1.59, 1.3.1.9, 2.3.1.38, 2.3.1.39, 3.1.2.14)protein42221% helix, 16% strandP07149
AFatty acid synthase subunit alpha (EC 2.3.1.86, 1.1.1.100, 2.3.1.41)protein16350% helix, 1% strandP19097

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13680.800.9074empty
210890.780.80114empty
37320.700.7774empty
41540.690.8949empty
5520.530.8919empty

Interfaces

1 interface between chains.

  • G–A · 42 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6WC7 · Acyl carrier protein (ACP) domain bound to dehydratase (DH) domain in fungal fatty acid… · the same entry in another collection · chain G against G, TM-score 1.00
  • P07149 · AlphaFold monomer V2.0 prediction for fatty acid synthase subunit beta (P07149) · a predicted model of the same protein · chain G against A, TM-score 0.95
  • P19097 · AlphaFold monomer V2.0 prediction for fatty acid synthase subunit alpha (P19097) · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

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