Research workbench
Crystal structure of staphylococcus aureus ketol-acid reductoisomerase in complex with mg, NADPH and inhibitor.
Analyse Crystal structure of staphylococcus aureus ketol-acid reductoisomerase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VO2
- Type
- protein
- Length
- 652 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ketol-acid reductoisomerase (NADP(+))
- EC
- 1.1.1.86
- UniProt
- A0A145BYP4
- Ligands
- R67, NDP, MG
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ketol-acid reductoisomerase (NADP(+)) (EC 1.1.1.86) | protein | 326 | 60% helix, 12% strand | A0A145BYP4 |
Ligands and binding sites
- R67 · 3-(methylsulfonyl)-2-oxopropanoic acid · ligand · 2 copies · chains A, B
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 445 | 0.75 | 0.84 | 55 | R67, MG, NDP |
| 2 | 406 | 0.75 | 0.85 | 51 | MG, NDP, R67 |
| 3 | 189 | 0.49 | 0.76 | 24 | empty |
| 4 | 59 | 0.34 | 0.78 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 6267 Ų buried · 56 hydrogen bonds · protein-protein
Compared structures
- 6VO2 · Crystal structure of Staphylococcus aureus ketol-acid reductoisomerase in complex with… · 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 A0A145BYP4
- Elsewhere: RCSB PDB 6VO2 · PDBe 6VO2 · UniProt A0A145BYP4
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