Research workbench
Electron cryomicroscopy structure of C. albicans fas in the ks-stalled state
Analyse Electron cryomicroscopy structure of C. albicans 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
- 6U5W
- Type
- protein
- Length
- 3,468 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
- P43098, P34731
- Ligands
- NAP, FMN
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 2 distinct chains · 42% helix, 17% 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 | 1435 | 47% helix, 14% strand | P43098 |
| 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 | 2033 | 38% helix, 18% strand | P34731 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- 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, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1157 | 0.78 | 0.80 | 92 | FMN, NAP |
| 2 | 413 | 0.74 | 0.84 | 46 | empty |
| 3 | 472 | 0.74 | 0.83 | 60 | NAP |
| 4 | 793 | 0.74 | 0.79 | 77 | empty |
| 5 | 176 | 0.71 | 0.88 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 5482 Ų buried · 68 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent, 2 cofactor (covalent ligand, flavinylation).
Compared structures
- 6U5W · Electron cryomicroscopy structure of C. albicans FAS in the KS-stalled state · the same entry in another collection · chain A against A, TM-score 1.00
- P34731 · AlphaFold monomer V2.0 prediction for fatty acid synthase subunit beta (P34731) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P43098 · AlphaFold monomer V2.0 prediction for fatty acid synthase subunit alpha (P43098) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P43098
- Every structure of UniProt P34731
- Elsewhere: RCSB PDB 6U5W · PDBe 6U5W · UniProt P43098 · UniProt P34731
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