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A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
Analyse A model for interfacial activation in lipases from the structure of a fungal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TGL
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase
- EC
- 3.1.1.3
- UniProt
- P19515
- Ligands
- HEE
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipase (EC 3.1.1.3) | protein | 265 | 0% helix, 0% strand | P19515 |
Ligands and binding sites
- HEE · N-hexylphosphonate ethyl ester · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.46 | 0.74 | 43 | empty |
| 2 | 98 | 0.37 | 0.73 | 19 | empty |
| 3 | 79 | 0.34 | 0.73 | 23 | empty |
| 4 | 79 | 0.32 | 0.73 | 29 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 P19515
- Elsewhere: RCSB PDB 5TGL · PDBe 5TGL · UniProt P19515
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