MolNFT v1 · #7153 · protein
Aspartyl dipeptidase (anisotropic B-factor refinement)
1FYE: “Aspartyl dipeptidase (anisotropic B-factor refinement)”. X-ray diffraction, 1 ligand (CD), 1 pocket (best druggability 0.33). MolNFT v1 #7153 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1FYE
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartyl dipeptidase
- EC
- 3.4.-.-
- UniProt
- P36936
- Ligands
- CD
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartyl dipeptidase (EC 3.4.-.-) | protein | 220 | 31% helix, 22% strand | P36936 |
Ligands and binding sites
- CD · Cadmium ion · metal · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.33 | 0.75 | 14 | empty |
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 P36936
- Elsewhere: RCSB PDB 1FYE · PDBe 1FYE · UniProt P36936
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