MolNFT v1 · #153400 · protein
Structure of a proline specific mutant of human cathepsin L
6JD8 · Cathepsin L1: “Structure of a proline specific mutant of human cathepsin L”. X-ray diffraction, 2 pockets (best druggability 0.51). MolNFT v1 #153400 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6JD8
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin L1
- EC
- 3.4.22.15
- UniProt
- P07711
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin L1 (EC 3.4.22.15) | protein | 314 | 33% helix, 18% strand | P07711 |
Ligands and binding sites
- EOH · Ethanol · additive · 12 copies · chains A
- GOL · Glycerol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PGE · Triethylene glycol · additive · chains A
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 | 77 | 0.51 | 0.84 | 17 | empty |
| 2 | 57 | 0.35 | 0.78 | 13 | EOH |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 P07711
- Elsewhere: RCSB PDB 6JD8 · PDBe 6JD8 · UniProt P07711
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