Research workbench
Campylobacter jejuni keto-acid reductoisomerase in complex with MG2+
Analyse Campylobacter jejuni keto-acid reductoisomerase in complex with MG2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LAT
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ketol-acid reductoisomerase
- UniProt
- A0A5T0UG45
- Ligands
- MG
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ketol-acid reductoisomerase | protein | 329 | 59% helix, 12% strand | A0A5T0UG45 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.49 | 0.73 | 31 | empty |
| 2 | 159 | 0.42 | 0.74 | 21 | MG |
| 3 | 82 | 0.36 | 0.76 | 20 | empty |
Compared structures
- 7LAT · Campylobacter jejuni keto-acid reductoisomerase in complex with Mg2+ · 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 A0A5T0UG45
- Elsewhere: RCSB PDB 7LAT · PDBe 7LAT · UniProt A0A5T0UG45
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