Research workbench
Cryo-EM structure of fatty acid synthase (fas) from pichia pastoris
Analyse Cryo-EM structure of fatty acid synthase (fas) from pichia pastoris in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BC4
- Type
- protein
- Length
- 3,514 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid synthase subunit alpha; Fatty acid synthase subunit beta
- EC
- 2.3.1.86, 1.1.1.100, 2.3.1.41, 4.2.1.59, 1.3.1.9, 2.3.1.38, 2.3.1.39, 3.1.2.14
- UniProt
- C4QY10, C4QVT8
- Ligands
- FMN
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 2 distinct chains · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid synthase subunit alpha (EC 2.3.1.86, 1.1.1.100, 2.3.1.41) | protein | 1460 | 41% helix, 14% strand | C4QY10 |
| B | Fatty 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) | protein | 2054 | 35% helix, 17% strand | C4QVT8 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1111 | 0.78 | 0.80 | 90 | FMN |
| 2 | 844 | 0.74 | 0.78 | 67 | empty |
| 3 | 207 | 0.73 | 0.89 | 32 | empty |
| 4 | 68 | 0.73 | 0.97 | 15 | empty |
| 5 | 465 | 0.71 | 0.81 | 55 | empty |
Interfaces
1 interface between chains.
- A–B · 5414 Ų buried · 60 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor (flavinylation).
Compared structures
- 7BC4 · Cryo-EM structure of fatty acid synthase (FAS) from Pichia pastoris · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt C4QY10
- Every structure of UniProt C4QVT8
- Elsewhere: RCSB PDB 7BC4 · PDBe 7BC4 · UniProt C4QY10 · UniProt C4QVT8
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