Research workbench
Crystal structure of human monoacylglycerol lipase in complex with compound 1
Analyse Crystal structure of human monoacylglycerol lipase in complex with compound 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L4T
- Type
- protein
- Length
- 576 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monoglyceride lipase
- UniProt
- A0A0C4DFN3
- Ligands
- XPD
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Monoglyceride lipase | protein | 288 | 42% helix, 17% strand | A0A0C4DFN3 |
Ligands and binding sites
- XPD · 6-{4-[(2-chloro-4-fluorophenoxy)methyl]piperidine-1-carbonyl}-2H-1,4-benzoxazin-3(4H)-one · ligand · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 4 copies · chains B, A
- ACT · Acetate ion · additive · 2 copies · chains A, B
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 | 513 | 0.75 | 0.83 | 52 | XPD |
| 2 | 467 | 0.74 | 0.83 | 45 | MPD |
| 3 | 367 | 0.60 | 0.76 | 38 | MPD |
| 4 | 110 | 0.43 | 0.78 | 17 | empty |
| 5 | 95 | 0.38 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 562 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7L4T · Crystal structure of human monoacylglycerol lipase in complex with compound 1 · 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 7L4T · PDBe 7L4T · UniProt A0A0C4DFN3
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