Research workbench
Structure of the mat domain of human fas
Analyse Structure of the mat domain of human fas in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JFD
- Type
- protein
- Length
- 1,606 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
- Pockets
- 18 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid synthase (EC 2.3.1.85) | protein | 404 | 44% helix, 16% strand | P49327 |
| B | Fatty acid synthase (EC 2.3.1.85) | protein | 400 | 44% helix, 16% strand | P49327 |
| C | Fatty acid synthase (EC 2.3.1.85) | protein | 403 | 45% helix, 16% strand | P49327 |
| D | Fatty acid synthase (EC 2.3.1.85) | protein | 399 | 45% helix, 16% strand | P49327 |
Pockets
18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.78 | 0.84 | 81 | empty |
| 2 | 60 | 0.70 | 0.97 | 23 | empty |
| 3 | 340 | 0.67 | 0.81 | 50 | empty |
| 4 | 336 | 0.66 | 0.80 | 51 | empty |
| 5 | 167 | 0.65 | 0.85 | 39 | empty |
Interfaces
3 interfaces between chains.
- C–D · 678 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 601 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 309 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 2JFD · PDBe 2JFD · UniProt P49327
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