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Crystal structure of an activation intermediate of cathepsin E
Analyse Crystal structure of an activation intermediate of cathepsin E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TZS
- Type
- protein
- Length
- 336 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin E; Activation peptide from cathepsin E; 23-mer peptide from pelb-IgG kappa…
- EC
- 3.4.23.34
- UniProt
- P14091
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin E (EC 3.4.23.34) | protein | 322 | 16% helix, 40% strand | P14091 |
| P | Activation peptide from cathepsin E (EC 3.4.23.34) | protein | 9 | 0% helix, 44% strand | P14091 |
| X | 23-mer peptide from pelb-IgG kappa light chain fusion protein | protein | 5 | 0% helix, 0% strand | — |
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 | 301 | 0.64 | 0.80 | 46 | empty |
| 2 | 119 | 0.40 | 0.75 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–P · 723 Ų buried · 14 hydrogen bonds · protein-protein
- P–X · 73 Ų buried · 3 hydrogen bonds · protein-protein
- A–X · 22 Ų buried · 0 hydrogen bonds · protein-protein
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 P14091
- Elsewhere: RCSB PDB 1TZS · PDBe 1TZS · UniProt P14091
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