MolNFT v1 · #178508 · protein
Processive cleavage of substrate at individual proteolytic active sites of the lon proteasecomplex (conformation 1)
7FID: “Processive cleavage of substrate at individual proteolytic active sites of the lon proteasecomplex…”. Electron microscopy, 2 ligands (AGS, ADP). MolNFT v1 #178508 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
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