Research workbench
Processive cleavage of substrate at individual proteolytic active sites of the lon proteasecomplex (conformation 1)
Analyse Processive cleavage of substrate at individual proteolytic active sites of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FID
- Type
- protein
- Length
- 4,696 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A059VAZ3
- Ligands
- AGS, ADP
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, C, D, E, F, A | — | protein | 779 | — | A0A059VAZ3 |
| S | — | protein | 22 | — | — |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 3 copies · chains B, C, D, A
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 A0A059VAZ3
- Elsewhere: RCSB PDB 7FID · PDBe 7FID · UniProt A0A059VAZ3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.