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Crystal structure of human monoglyceride lipase
Analyse Crystal structure of human monoglyceride lipase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HJU
- Type
- protein
- Length
- 582 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monoglyceride lipase
- EC
- 3.1.1.23
- UniProt
- Q99685
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monoglyceride lipase (EC 3.1.1.23) | protein | 291 | 41% helix, 17% strand | Q99685 |
| B | Monoglyceride lipase (EC 3.1.1.23) | protein | 291 | 40% helix, 17% strand | Q99685 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 520 | 0.77 | 0.84 | 47 | GOL |
| 2 | 491 | 0.76 | 0.84 | 48 | GOL |
| 3 | 160 | 0.65 | 0.86 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 925 Ų buried · 10 hydrogen bonds · protein-protein
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 Q99685
- Elsewhere: RCSB PDB 3HJU · PDBe 3HJU · UniProt Q99685
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