Research workbench
Structure of the human fatty acid synthase ks-mat didomain as a framework for inhibitor design.
Analyse Structure of the human fatty acid synthase ks-mat didomain as a framework for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HHD
- Type
- protein
- Length
- 3,413 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid synthase
- EC
- 2.3.1.85
- UniProt
- P49327
- Ligands
- CL
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fatty acid synthase (EC 2.3.1.85) | protein | 852 | 39% helix, 18% strand | P49327 |
| C | Fatty acid synthase (EC 2.3.1.85) | protein | 855 | 39% helix, 18% strand | P49327 |
| D | Fatty acid synthase (EC 2.3.1.85) | protein | 854 | 39% helix, 18% strand | P49327 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 482 | 0.84 | 0.91 | 79 | empty |
| 2 | 125 | 0.78 | 0.97 | 32 | empty |
| 3 | 122 | 0.76 | 0.96 | 32 | empty |
| 4 | 163 | 0.68 | 0.88 | 31 | empty |
| 5 | 167 | 0.67 | 0.87 | 30 | empty |
Interfaces
3 interfaces between chains.
- A–D · 2787 Ų buried · 34 hydrogen bonds · protein-protein
- B–C · 2777 Ų buried · 34 hydrogen bonds · protein-protein
- A–B · 532 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3HHD · Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor… · the same entry in another collection · chain D against D, TM-score 1.00
- P49327 · AlphaFold monomer V2.0 prediction for fatty acid synthase (P49327) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P49327
- Elsewhere: RCSB PDB 3HHD · PDBe 3HHD · UniProt P49327
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