Research workbench
Turning an asparaginyl endopeptidase into a peptide ligase
Analyse Turning an asparaginyl endopeptidase into a peptide ligase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L4V
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0P0QM28
- Ligands
- SNN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 414 | — | A0A0P0QM28 |
Ligands and binding sites
- SNN · L-3-aminosuccinimide · ligand · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6L4V · 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 6L4V · PDBe 6L4V · UniProt A0A0P0QM28
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