MolNFT v2 · #125262 · protein
Dihydrodipicolinate reductase from the industrial and evolutionarily important cyanobacteria Anabaena variabilis.
5KT0: “Dihydrodipicolinate reductase from the industrial and evolutionarily important cyanobacteria Anabaena…”. X-ray diffraction at 2.83, 1 ligand (MG). MolNFT v2 #125262 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5KT0
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.83
- Source
- Anabaena variabilis (strain ATCC 29413 / PCC 7937)
- UniProt
- Q3MFY8
- Ligands
- MG
Structure
x-ray diffraction · resolution 2.83 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 274 | — | Q3MFY8 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5KT0 · Dihydrodipicolinate reductase from the industrial and evolutionarily important… · the same entry in another collection · chain A against A, TM-score 1.00
- Q3MFY8 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate reductase (Q3MFY8) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q3MFY8
- Elsewhere: RCSB PDB 5KT0 · PDBe 5KT0 · UniProt Q3MFY8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.