Research workbench
Eiav protease complexed with the inhibitor hby-793
Analyse Eiav protease complexed with the inhibitor hby-793 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FMB
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eiav protease
- EC
- 3.4.23.16
- UniProt
- P32542
- Ligands
- HYB
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eiav protease (EC 3.4.23.16) | protein | 104 | 12% helix, 43% strand | P32542 |
Ligands and binding sites
- HYB · [2-(2-methyl-propane-2-sulfonylmethyl)-3-naphthalen-1-yl-propionyl-valinyl]-phenylalaninol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.48 | 0.76 | 22 | empty |
| 2 | 62 | 0.28 | 0.73 | 16 | empty |
Compared structures
- 1FMB · Eiav protease complexed with the inhibitor hby-793 · 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 P32542
- Elsewhere: RCSB PDB 1FMB · PDBe 1FMB · UniProt P32542
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