Research workbench
Structure of mutant human cathepsin L, engineered for gag binding
Analyse Structure of mutant human cathepsin L, engineered for gag binding in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JD0
- 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
- Ligands
- NA, PO4, CL
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin L1 (EC 3.4.22.15) | protein | 314 | 34% helix, 18% strand | P07711 |
Ligands and binding sites
- NA · Sodium ion · metal · 5 copies · chains A
- PO4 · Phosphate ion · ion · 8 copies · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 14 copies · chains A
- POL · N-propanol · additive · 10 copies · chains A
- PGE · Triethylene glycol · additive · 6 copies · chains A
- EOH · Ethanol · additive · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
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 | 111 | 0.52 | 0.82 | 26 | GOL |
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 6JD0 · PDBe 6JD0 · UniProt P07711
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