Research workbench
Structure of digestive procathepsin L2 proteinase from tenebrio molitor larval midgut
Analyse Structure of digestive procathepsin L2 proteinase from tenebrio molitor larval… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QJ3
- Type
- protein
- Length
- 634 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin L-like protein
- EC
- 3.4.22.15
- UniProt
- Q69G21
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin L-like protein (EC 3.4.22.15) | protein | 319 | 35% helix, 19% strand | Q69G21 |
| B | Cathepsin L-like protein (EC 3.4.22.15) | protein | 315 | 35% helix, 19% strand | Q69G21 |
Ligands and binding sites
- ACT · Acetate ion · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 975 | 0.76 | 0.79 | 98 | ACT |
Interfaces
1 interface between chains.
- A–B · 704 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 3QJ3 · Structure of digestive procathepsin L2 proteinase from Tenebrio molitor larval midgut · 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 Q69G21
- Elsewhere: RCSB PDB 3QJ3 · PDBe 3QJ3 · UniProt Q69G21
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