MolNFT v1 · #91449 · protein
Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic locally isolated bacillus sp. L2.
4FDM · Thermostable lipase: “Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic locally isolated…”. X-ray diffraction, 2 ligands (ZN, CA), 2 pockets (best druggability 0.52). MolNFT v1 #91449 on…
- 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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