Research workbench
Clpx in clpx-clpp complex bound to substrate and ATP-gamma-S, class 3
Analyse Clpx in clpx-clpp complex bound to substrate and ATP-gamma-S, class 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PP6
- Type
- protein
- Length
- 2,068 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1Q9L861
- Ligands
- AGS, ADP
Structure
electron microscopy · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 344 | — | A0A1Q9L861 |
| B | — | protein | 346 | — | A0A1Q9L861 |
| C | — | protein | 346 | — | A0A1Q9L861 |
| D | — | protein | 349 | — | A0A1Q9L861 |
| E | — | protein | 345 | — | A0A1Q9L861 |
| F | — | protein | 331 | — | A0A1Q9L861 |
| S | — | protein | 7 | — | — |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 5 copies · chains A, B, C, D, E, F
- ADP · Adenosine-5'-diphosphate · ligand · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PP6 · ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 3 · 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 A0A1Q9L861
- Elsewhere: RCSB PDB 6PP6 · PDBe 6PP6 · UniProt A0A1Q9L861
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