Research workbench
Arabidopsis thaliana acetohydroxyacid synthase complex
Analyse Arabidopsis thaliana acetohydroxyacid synthase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U9H
- Type
- protein
- Length
- 5,952 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetolactate synthase, chloroplastic; Acetolactate synthase small subunit 2, chloroplastic
- EC
- 2.2.1.6
- UniProt
- P17597, Q93YZ7
- Ligands
- FAD, TPP, MG
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 32% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, H, I, L, M, P, Q | Acetolactate synthase, chloroplastic (EC 2.2.1.6) | protein | 582 | 33% helix, 13% strand | P17597 |
| F, J, N, R | Acetolactate synthase small subunit 2, chloroplastic | protein | 155 | 30% helix, 30% strand | Q93YZ7 |
| G, K, O, S | Acetolactate synthase small subunit 2, chloroplastic | protein | 169 | 30% helix, 33% strand | Q93YZ7 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 8 copies · chains A, B, H, I, L, M, P, Q
- TPP · Thiamine diphosphate · ligand · 8 copies · chains A, B, H, I, L, M, P, Q
- MG · Magnesium ion · metal · 8 copies · chains A, B, H, I, L, M, P, Q
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 | 438 | 0.87 | 0.94 | 82 | MG, FAD, TPP |
| 2 | 508 | 0.86 | 0.93 | 91 | MG, FAD, TPP |
| 3 | 414 | 0.86 | 0.94 | 80 | MG, FAD, TPP |
| 4 | 415 | 0.86 | 0.94 | 80 | MG, FAD, TPP |
| 5 | 490 | 0.86 | 0.93 | 86 | MG, FAD, TPP |
Interfaces
38 interfaces between chains.
- A–B · 3692 Ų buried · 42 hydrogen bonds · protein-protein
- P–Q · 3686 Ų buried · 37 hydrogen bonds · protein-protein
- L–M · 3681 Ų buried · 37 hydrogen bonds · protein-protein
- H–I · 3678 Ų buried · 37 hydrogen bonds · protein-protein
- N–O · 2698 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 6U9H · Arabidopsis thaliana acetohydroxyacid synthase complex · the same entry in another collection · chain S against S, 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 P17597
- Every structure of UniProt Q93YZ7
- Elsewhere: RCSB PDB 6U9H · PDBe 6U9H · UniProt P17597 · UniProt Q93YZ7
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