Research workbench
The active site of aspartic proteinases
Analyse The active site of aspartic proteinases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ER3
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothiapepsin
- EC
- 3.4.23.6
- UniProt
- P11838
- Ligands
- 0EL
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Endothiapepsin (EC 3.4.23.6) | protein | 330 | 12% helix, 44% strand | P11838 |
Ligands and binding sites
- 0EL · 6-ammonio-N-[(2R,4R,5R)-5-{[N-(tert-butoxycarbonyl)-L-phenylalanyl-3-(1H-imidazol-3-ium-4-yl)-L-alanyl]amino}-6-cyclohexyl-4-hydroxy-2-(2-methylpropyl)hexanoyl]-L-norleucylphenylalanine · ligand · chains E
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 | 309 | 0.59 | 0.78 | 36 | 0EL |
Modifications
Observed in the structure: 1 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 P11838
- Elsewhere: RCSB PDB 3ER3 · PDBe 3ER3 · UniProt P11838
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