Research workbench
Homo sapiens fatty acid synthetase, thioesterase domain at 1.7 ångströms resolution
Analyse Homo sapiens fatty acid synthetase, thioesterase domain at 1.7 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Z49
- Type
- protein
- Length
- 544 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid synthase
- EC
- 3.1.2.14
- UniProt
- P49327
- Ligands
- K
- Pockets
- 6 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid synthase (EC 3.1.2.14) | protein | 262 | 44% helix, 13% strand | P49327 |
| B | Fatty acid synthase (EC 3.1.2.14) | protein | 282 | 45% helix, 12% strand | P49327 |
Ligands and binding sites
- K · Potassium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.59 | 0.79 | 29 | empty |
| 2 | 81 | 0.40 | 0.78 | 19 | K |
| 3 | 115 | 0.37 | 0.73 | 15 | empty |
| 4 | 71 | 0.33 | 0.75 | 14 | empty |
| 5 | 83 | 0.33 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 758 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4Z49 · Homo Sapiens Fatty Acid Synthetase, Thioesterase Domain at 1.7 Angstroms Resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P49327 · AlphaFold monomer V2.0 prediction for fatty acid synthase (P49327) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 4Z49 · PDBe 4Z49 · UniProt P49327
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