Research workbench
Saccharomyces cerevisiae fas type I
Analyse Saccharomyces cerevisiae fas type I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HMJ
- Type
- protein
- Length
- 11,349 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid synthase subunit alpha; Fatty acid synthase subunit beta
- EC
- 2.3.1.86
- UniProt
- P19097, P07149
- Ligands
- CER, FMN
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Fatty acid synthase subunit alpha (EC 2.3.1.86) | protein | 1750 | 46% helix, 15% strand | P19097 |
| G, H, I | Fatty acid synthase subunit beta (EC 2.3.1.86) | protein | 2033 | 41% helix, 19% strand | P07149 |
Ligands and binding sites
- CER · (2S, 3R)-3-hydroxy-4-oxo-7,10-trans,trans-dodecadienamide · ligand · 3 copies · chains A, B, C
- FMN · Flavin mononucleotide · ligand · 3 copies · chains G, H, I
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 | 1067 | 0.79 | 0.80 | 76 | FMN |
| 2 | 1047 | 0.79 | 0.80 | 85 | FMN |
| 3 | 1057 | 0.79 | 0.80 | 84 | FMN |
| 4 | 673 | 0.75 | 0.81 | 87 | empty |
| 5 | 1089 | 0.73 | 0.76 | 95 | empty |
Interfaces
12 interfaces between chains.
- A–G · 5469 Ų buried · 71 hydrogen bonds · protein-protein
- C–I · 5468 Ų buried · 73 hydrogen bonds · protein-protein
- B–H · 5457 Ų buried · 73 hydrogen bonds · protein-protein
- A–C · 917 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 910 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
- 3HMJ · Saccharomyces cerevisiae FAS type I · the same entry in another collection · chain I against I, 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 I 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 B against A, TM-score 0.85
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 P19097
- Every structure of UniProt P07149
- Elsewhere: RCSB PDB 3HMJ · PDBe 3HMJ · UniProt P19097 · UniProt P07149
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