MolNFT v1 · #14597 · protein
Crystal structure of a caricain D158E mutant in complex with E-64
1MEG: “Crystal structure of a caricain D158E mutant in complex with E-64”. X-ray diffraction, 1 ligand (E64), 1 pocket (best druggability 0.28). MolNFT v1 #14597 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MEG
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caricain
- EC
- 3.4.22.30
- UniProt
- P10056
- Ligands
- E64
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caricain (EC 3.4.22.30) | protein | 216 | 26% helix, 25% strand | P10056 |
Ligands and binding sites
- E64 · N-[N-[1-hydroxycarboxyethyl-carbonyl]leucylamino-butyl]-guanidine · ligand · chains A
- EOH · Ethanol · additive · 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 | 50 | 0.28 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).
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 P10056
- Elsewhere: RCSB PDB 1MEG · PDBe 1MEG · UniProt P10056
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