MolNFT v1 · #76380 · protein

Structure of digestive procathepsin L2 proteinase from tenebrio molitor larval midgut

3QJ3 · Cathepsin L-like protein: “Structure of digestive procathepsin L2 proteinase from tenebrio molitor larval midgut”. X-ray diffraction, 1 pocket (best druggability 0.76). MolNFT v1 #76380 on GenesisL1: 3D structure, binding sites and…

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	975	0.76	0.79	98	ACT

Interfaces

1 interface between chains.

A–B · 704 Å² 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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