Research workbench
Crystal structure of human monoacylglycerol lipase in complex with compound 1H
Analyse Crystal structure of human monoacylglycerol lipase in complex with compound 1H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L4U
- Type
- protein
- Length
- 572 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monoglyceride lipase
- UniProt
- A0A0C4DFN3
- Ligands
- XP7, CL
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monoglyceride lipase | protein | 285 | 40% helix, 18% strand | A0A0C4DFN3 |
| B | Monoglyceride lipase | protein | 287 | 38% helix, 17% strand | A0A0C4DFN3 |
Ligands and binding sites
- XP7 · (5S)-5-(3-{4-[(2-chloro-4-fluorophenoxy) methyl]piperidin-1-yl}-3-oxopropyl)pyrrolidin-2-one · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 535 | 0.74 | 0.82 | 48 | XP7 |
| 2 | 396 | 0.66 | 0.79 | 46 | XP7 |
| 3 | 389 | 0.60 | 0.76 | 31 | empty |
| 4 | 123 | 0.45 | 0.78 | 28 | empty |
| 5 | 82 | 0.37 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 547 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7L4U · Crystal structure of human monoacylglycerol lipase in complex with compound 1h · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A0C4DFN3
- Elsewhere: RCSB PDB 7L4U · PDBe 7L4U · UniProt A0A0C4DFN3
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