MolNFT v1 · #29007 · protein
Acetohydroxy acid isomeroreductase complexed with NADPH, magnesium and inhibitor ipoha (N-hydroxy-N- isopropyloxamate)
1YVE: “Acetohydroxy acid isomeroreductase complexed with NADPH, magnesium and inhibitor ipoha (N-hydroxy-N…”. X-ray diffraction, 4 ligands (NDP, HIO, MG), 20 pockets (best druggability 0.78). MolNFT v1 #29007 on GenesisL1: 3D structure…
- PDB
- 1YVE
- Type
- protein
- Length
- 2,046 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetohydroxy acid isomeroreductase
- EC
- 1.1.1.86
- UniProt
- Q01292
- Ligands
- NDP, HIO, MG, CL
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| I, L | Acetohydroxy acid isomeroreductase (EC 1.1.1.86) | protein | 513 | 58% helix, 11% strand | Q01292 |
| J, K | Acetohydroxy acid isomeroreductase (EC 1.1.1.86) | protein | 510 | 57% helix, 11% strand | Q01292 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains I, K, L, J
- HIO · N-hydroxy-N-isopropyloxamic acid · ligand · 4 copies · chains I, J, K, L
- MG · Magnesium ion · metal · 8 copies · chains I, J, K, L
- CL · Chloride ion · ion · 3 copies · chains I, J, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.78 | 0.96 | 30 | empty |
| 2 | 132 | 0.78 | 0.96 | 32 | empty |
| 3 | 136 | 0.78 | 0.96 | 31 | empty |
| 4 | 136 | 0.78 | 0.96 | 30 | empty |
| 5 | 566 | 0.77 | 0.84 | 63 | MG, NDP, HIO |
Interfaces
4 interfaces between chains.
- I–J · 2190 Ų buried · 15 hydrogen bonds · protein-protein
- K–L · 2162 Ų buried · 18 hydrogen bonds · protein-protein
- J–L · 536 Ų buried · 8 hydrogen bonds · protein-protein
- I–K · 528 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1YVE · Acetohydroxy acid isomeroreductase complexed with NADPH, magnesium and inhibitor ipoha… · the same entry in another collection · chain I against I, TM-score 1.00
- Q01292 · AlphaFold monomer V2.0 prediction for ketol-acid reductoisomerase, chloroplastic (Q01292) · a predicted model of the same protein · chain J 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 Q01292
- Elsewhere: RCSB PDB 1YVE · PDBe 1YVE · UniProt Q01292
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