MolNFT v1 · #143900 · protein
Saccharomyces cerevisiae acetohydroxyacid synthase
6BD9 · Acetolactate synthase catalytic subunit, mitochondrial: “Saccharomyces cerevisiae acetohydroxyacid synthase”. X-ray diffraction, 7 ligands (PYR, FAD, TPP), 11 pockets (best druggability 0.84). MolNFT v1 #143900 on GenesisL1: 3D…
- PDB
- 6BD9
- Type
- protein
- Length
- 1,106 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetolactate synthase catalytic subunit, mitochondrial
- EC
- 2.2.1.6
- UniProt
- P07342
- Ligands
- PYR, FAD, TPP, K, MG, OXY, PO4
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetolactate synthase catalytic subunit, mitochondrial (EC 2.2.1.6) | protein | 542 | 45% helix, 18% strand | P07342 |
| B | Acetolactate synthase catalytic subunit, mitochondrial (EC 2.2.1.6) | protein | 564 | 41% helix, 18% strand | P07342 |
Ligands and binding sites
- PYR · Pyruvic acid · ligand · 4 copies · chains A, B
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- TPP · Thiamine diphosphate · ligand · 2 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- OXY · Oxygen molecule · ion · 8 copies · chains A, B
- PO4 · Phosphate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1102 | 0.84 | 0.85 | 126 | PYR, OXY, FAD, MG, TPP |
| 2 | 1098 | 0.81 | 0.82 | 126 | MG, FAD, TPP, OXY, PYR |
| 3 | 58 | 0.43 | 0.83 | 15 | empty |
| 4 | 129 | 0.40 | 0.75 | 16 | empty |
| 5 | 121 | 0.37 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2306 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
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 P07342
- Elsewhere: RCSB PDB 6BD9 · PDBe 6BD9 · UniProt P07342
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