MolNFT v1 · #60834 · protein
Crystal structure of LIPASE/ESTERASE (LP_2923) from lactobacillus plantarum. northeast structural genomics consortium target LPR108
3D3N · Putative LIPASE/ESTERASE: “Crystal structure of LIPASE/ESTERASE (LP_2923) from lactobacillus plantarum. northeast structural genomics…”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.44). MolNFT v1 #60834 on…
- PDB
- 3D3N
- Type
- protein
- Length
- 499 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative LIPASE/ESTERASE
- UniProt
- Q88TL9
- Ligands
- CA
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative LIPASE/ESTERASE | protein | 245 | 34% helix, 23% strand | Q88TL9 |
| B | Putative LIPASE/ESTERASE | protein | 254 | 30% helix, 22% strand | Q88TL9 |
Ligands and binding sites
- CA · Calcium ion · metal · chains B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.44 | 0.78 | 26 | empty |
| 2 | 68 | 0.30 | 0.74 | 18 | empty |
| 3 | 54 | 0.27 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 932 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3D3N · Crystal structure of lipase/esterase (lp_2923) from Lactobacillus plantarum. Northeast… · 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 Q88TL9
- Elsewhere: RCSB PDB 3D3N · PDBe 3D3N · UniProt Q88TL9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.