Research workbench
Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by orlistat
Analyse Crystal structure of the thioesterase domain of human fatty acid synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PX6
- Type
- protein
- Length
- 516 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49327
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 253 | — | P49327 |
| B | — | protein | 263 | — | P49327 |
Compared structures
- 2PX6 · Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by… · 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 0.97
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 2PX6 · PDBe 2PX6 · UniProt P49327
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