MolNFT v2 · #4215 · protein
An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase
1DGE: “An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase”. X-ray diffraction at 2.8. MolNFT v2 #4215 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DGE
- Type
- protein
- Length
- 431 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.8
- Source
- Burkholderia cepacia
- UniProt
- P16932
Structure
x-ray diffraction · resolution 2.8 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 431 | — | P16932 |
Compared structures
- 1DGE · An alkali metal ion size-dependent switch in the active site structure of dialkylglycine… · the same entry in another collection · chain A against A, TM-score 1.00
- P16932 · AlphaFold monomer V2.0 prediction for 2,2-dialkylglycine decarboxylase (P16932) · a predicted model of the same protein · 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 P16932
- Elsewhere: RCSB PDB 1DGE · PDBe 1DGE · UniProt P16932
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.