Research workbench
Structure of cpii bound to ADP, AMP and acetate, from thiomonas intermedia K12
Analyse Structure of cpii bound to ADP, AMP and acetate, from thiomonas intermedia K12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D4N
- Type
- protein
- Length
- 293 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D5X329
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 105 | — | D5X329 |
| B | — | protein | 90 | — | D5X329 |
| C | — | protein | 98 | — | D5X329 |
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 D5X329
- Elsewhere: RCSB PDB 5D4N · PDBe 5D4N · UniProt D5X329
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.