MolNFT v1 · #14095 · protein
Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design
1LYA: “Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting…”. X-ray diffraction, 3 ligands (NAG, BMA, MAN), 4 pockets (best druggability 0.69). MolNFT v1 #14095 on GenesisL1: 3D…
- PDB
- 1LYA
- Type
- protein
- Length
- 676 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin D
- EC
- 3.4.23.5
- UniProt
- P07339
- Ligands
- NAG, BMA, MAN
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Cathepsin D (EC 3.4.23.5) | protein | 97 | 7% helix, 55% strand | P07339 |
| B, D | Cathepsin D (EC 3.4.23.5) | protein | 241 | 15% helix, 43% strand | P07339 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B, C, D
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains B, D
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 639 | 0.69 | 0.77 | 51 | empty |
| 2 | 542 | 0.66 | 0.76 | 47 | empty |
| 3 | 370 | 0.57 | 0.75 | 49 | empty |
| 4 | 81 | 0.32 | 0.74 | 20 | empty |
Interfaces
4 interfaces between chains.
- A–B · 3280 Ų buried · 84 hydrogen bonds · protein-protein
- C–D · 3271 Ų buried · 80 hydrogen bonds · protein-protein
- B–D · 159 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 79 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 1LYA · Crystal structures of native and inhibited forms of human cathepsin D: implications for… · the same entry in another collection · chain D against D, TM-score 1.00
- P07339 · AlphaFold monomer V2.0 prediction for cathepsin D (P07339) · a predicted model of the same protein · chain D against A, TM-score 0.99
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 P07339
- Elsewhere: RCSB PDB 1LYA · PDBe 1LYA · UniProt P07339
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