Research workbench
Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic locally isolated bacillus sp. L2.
Analyse Crystallization and 3D structure elucidation of thermostable L2 lipase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FDM
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermostable lipase
- EC
- 3.1.1.3
- UniProt
- Q5I4I3
- Ligands
- ZN, CA
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thermostable lipase (EC 3.1.1.3) | protein | 378 | 40% helix, 16% strand | Q5I4I3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.52 | 0.77 | 21 | empty |
| 2 | 67 | 0.31 | 0.74 | 16 | empty |
Compared structures
- 4FDM · Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic… · 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 Q5I4I3
- Elsewhere: RCSB PDB 4FDM · PDBe 4FDM · UniProt Q5I4I3
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