Research workbench
Crystal structure of the cysteine protease inhibitor, EHICP2, from entamoeba histolytica
Analyse Crystal structure of the cysteine protease inhibitor, EHICP2, from entamoeba… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M88
- Type
- protein
- Length
- 213 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amoebiasin-2
- UniProt
- C4M2H5
- Ligands
- CL, SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amoebiasin-2 | protein | 110 | 5% helix, 55% strand | C4M2H5 |
| B | Amoebiasin-2 | protein | 103 | 6% helix, 59% strand | C4M2H5 |
Ligands and binding sites
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 | 67 | 0.29 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 510 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3M88 · Crystal structure of the cysteine protease inhibitor, EhICP2, from Entamoeba histolytica · the same entry in another collection · chain A against A, TM-score 1.00
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 C4M2H5
- Elsewhere: RCSB PDB 3M88 · PDBe 3M88 · UniProt C4M2H5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.