Research workbench
Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 ångström resolution
Analyse Crystal structure of yeast fatty acid synthase with stalled acyl carrier… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UV8
- Type
- protein
- Length
- 10,941 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid synthase subunit alpha (FAS2); Fatty acid synthase subunit beta (FAS1)
- EC
- 2.3.1.86
- UniProt
- P19097, P07149
- Ligands
- FMN
- Pockets
- 20 · best druggability 0.80
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 (FAS2) (EC 2.3.1.86) | protein | 1614 | 48% helix, 14% strand | P19097 |
| G, H, I | Fatty acid synthase subunit beta (FAS1) (EC 2.3.1.86) | protein | 2033 | 41% helix, 19% strand | P07149 |
Ligands and binding sites
- 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 | 1097 | 0.80 | 0.81 | 83 | FMN |
| 2 | 1063 | 0.79 | 0.80 | 90 | FMN |
| 3 | 1112 | 0.78 | 0.80 | 85 | FMN |
| 4 | 757 | 0.76 | 0.80 | 86 | empty |
| 5 | 784 | 0.76 | 0.80 | 88 | empty |
Interfaces
12 interfaces between chains.
- B–H · 5566 Ų buried · 80 hydrogen bonds · protein-protein
- C–I · 5556 Ų buried · 79 hydrogen bonds · protein-protein
- A–G · 5515 Ų buried · 74 hydrogen bonds · protein-protein
- A–C · 1045 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1035 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (nonstandard).
Compared structures
- 2UV8 · Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1… · the same entry in another collection · chain H against H, 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 H 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 0.87
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 2UV8 · PDBe 2UV8 · UniProt P19097 · UniProt P07149
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