MolNFT v1 · #155354 · protein
Turning an asparaginyl endopeptidase into a peptide ligase
6L4X: “Turning an asparaginyl endopeptidase into a peptide ligase”. X-ray diffraction, 1 ligand (SNN), 3 pockets (best druggability 0.51). MolNFT v1 #155354 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6L4X
- Type
- protein
- Length
- 412 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Asparaginyl endopeptidase
- EC
- 3.4.22.34
- UniProt
- A0A0P0QM28
- Ligands
- SNN
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Asparaginyl endopeptidase (EC 3.4.22.34) | protein | 412 | 42% helix, 12% strand | A0A0P0QM28 |
Ligands and binding sites
- SNN · L-3-aminosuccinimide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.51 | 0.79 | 26 | empty |
| 2 | 64 | 0.42 | 0.81 | 18 | empty |
| 3 | 132 | 0.41 | 0.75 | 20 | empty |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6L4X · Turning an asparaginyl endopeptidase into a peptide ligase · 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 A0A0P0QM28
- Elsewhere: RCSB PDB 6L4X · PDBe 6L4X · UniProt A0A0P0QM28
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