Research workbench
X-ray studies of aspartic proteinase-statine inhibitor complexes
Analyse X-ray studies of aspartic proteinase-statine inhibitor complexes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ER0
- Type
- protein
- Length
- 336 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothiapepsin; L364,099
- EC
- 3.4.23.6
- UniProt
- P11838
- Ligands
- IVA
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Endothiapepsin (EC 3.4.23.6) | protein | 330 | 10% helix, 46% strand | P11838 |
| I | L364,099 | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- IVA · Isovaleric acid · ligand · chains E, I
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 | 58 | 0.31 | 0.75 | 18 | IVA |
Interfaces
1 interface between chains.
- E–I · 694 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 disulfide, 1 modified (covalent ligand, disulfide, nonstandard).
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 2ER0 · PDBe 2ER0 · UniProt P11838
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