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Crystal structure of monoacylglycerol lipase from thermophilic geobacillus sp. 12AMOR
Analyse Crystal structure of monoacylglycerol lipase from thermophilic geobacillus sp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XKS
- Type
- protein
- Length
- 1,510 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermostable monoacylglycerol lipase
- EC
- 3.1.1.23
- UniProt
- A0A0G3XXB4
- Pockets
- 15 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Thermostable monoacylglycerol lipase (EC 3.1.1.23) | protein | 252 | 41% helix, 17% strand | A0A0G3XXB4 |
| B, D, E | Thermostable monoacylglycerol lipase (EC 3.1.1.23) | protein | 251 | 41% helix, 17% strand | A0A0G3XXB4 |
| F | Thermostable monoacylglycerol lipase (EC 3.1.1.23) | protein | 253 | 40% helix, 17% strand | A0A0G3XXB4 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 853 | 0.80 | 0.83 | 87 | empty |
| 2 | 577 | 0.71 | 0.79 | 63 | empty |
| 3 | 271 | 0.68 | 0.83 | 34 | empty |
| 4 | 245 | 0.66 | 0.83 | 33 | empty |
| 5 | 297 | 0.64 | 0.80 | 32 | empty |
Interfaces
7 interfaces between chains.
- D–E · 440 Ų buried · 1 hydrogen bond · protein-protein
- A–F · 393 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 286 Ų buried · 0 hydrogen bonds · protein-protein
- A–E · 183 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 181 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5XKS · Crystal structure of monoacylglycerol lipase from thermophilic Geobacillus sp. 12AMOR · 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 A0A0G3XXB4
- Elsewhere: RCSB PDB 5XKS · PDBe 5XKS · UniProt A0A0G3XXB4
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