Research workbench
Electron cryomicroscopy structure of S. cerevisiae fas in the ks- stalled state
Analyse Electron cryomicroscopy structure of S. cerevisiae fas in the ks- stalled state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U5U
- Type
- protein
- Length
- 3,644 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
- A0A140KF01, P07149
- Ligands
- NAP, PNS, FMN
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 2 distinct chains · 41% helix, 15% 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 | 1611 | 45% helix, 10% strand | A0A140KF01 |
| G | 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 | 2033 | 38% helix, 19% strand | P07149 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, G
- PNS · 4'-phosphopantetheine · ligand · chains A
- FMN · Flavin mononucleotide · ligand · chains G
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 | 1055 | 0.79 | 0.80 | 99 | FMN, NAP |
| 2 | 1089 | 0.76 | 0.79 | 111 | empty |
| 3 | 664 | 0.76 | 0.81 | 72 | empty |
| 4 | 422 | 0.75 | 0.85 | 43 | empty |
| 5 | 724 | 0.74 | 0.80 | 73 | NAP |
Interfaces
1 interface between chains.
- A–G · 5464 Ų buried · 70 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 covalent, 1 cofactor (covalent ligand, phosphopantetheinylation).
Compared structures
- 6U5U · Electron cryomicroscopy Structure of S. cerevisiae FAS in the KS-stalled state · the same entry in another collection · chain A against A, 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 0.93
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 A0A140KF01
- Every structure of UniProt P07149
- Elsewhere: RCSB PDB 6U5U · PDBe 6U5U · UniProt A0A140KF01 · UniProt P07149
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