Research workbench
Crystal structure of Monoacylglycerol Lipase chimera
Analyse Crystal structure of Monoacylglycerol Lipase chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E0N
- Type
- protein
- Length
- 1,004 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Bacillus oceanisediminis 2691; Geobacillus sp. 12AMOR1
- Molecule
- Thermostable monoacylglycerol lipase,Lipase
- UniProt
- A0A160MIM0
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · resolution 1.85 · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Thermostable monoacylglycerol lipase,Lipase | protein | 251 | 40% helix, 17% strand | A0A160MIM0 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 521 | 0.79 | 0.86 | 45 | empty |
| 2 | 491 | 0.77 | 0.85 | 42 | empty |
| 3 | 193 | 0.61 | 0.82 | 29 | empty |
| 4 | 304 | 0.57 | 0.77 | 34 | empty |
| 5 | 50 | 0.29 | 0.75 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–B · 648 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 556 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 555 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7E0N · Crystal structure of monoacylglycerol lipase chimera · 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 A0A160MIM0
- Elsewhere: RCSB PDB 7E0N · PDBe 7E0N · UniProt A0A160MIM0
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