MolNFT v1 · #167900 · protein

Arabidopsis thaliana acetohydroxyacid synthase complex with valine bound

6VZ8 · Acetolactate synthase, chloroplastic: “Arabidopsis thaliana acetohydroxyacid synthase complex with valine bound”. Electron microscopy, 4 ligands (FAD, TPP, VAL), 20 pockets (best druggability 0.88). MolNFT v1 #167900 on GenesisL1…

PDB: 6VZ8
Type: protein
Length: 5,560 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, VAL, MG
Pockets: 20 · best druggability 0.88

Structure

electron microscopy · 4 distinct chains · 39% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D, H, L, P	Acetolactate synthase, chloroplastic (EC 2.2.1.6)	protein	531	41% helix, 16% strand	P17597
E, I, M, Q	Acetolactate synthase, chloroplastic (EC 2.2.1.6)	protein	541	41% helix, 17% strand	P17597
F, J, N, R	Acetolactate synthase small subunit 2, chloroplastic	protein	159	31% helix, 43% strand	Q93YZ7
G, K, O, S	Acetolactate synthase small subunit 2, chloroplastic	protein	159	30% helix, 40% strand	Q93YZ7

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 8 copies · chains D, E, H, I, L, M, P, Q
TPP · Thiamine diphosphate · ligand · 8 copies · chains D, E, H, I, L, M, P, Q
VAL · Valine · ligand · 8 copies · chains F, G, J, K, N, O, R, S
MG · Magnesium ion · metal · 8 copies · chains D, E, 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	797	0.88	0.91	113	empty
2	629	0.88	0.93	92	empty
3	930	0.88	0.90	116	empty
4	883	0.87	0.89	118	MG, FAD, TPP
5	825	0.86	0.89	102	MG, FAD, TPP

Interfaces

36 interfaces between chains.

P–Q · 2737 Å² buried · 13 hydrogen bonds · protein-protein
D–E · 2726 Å² buried · 13 hydrogen bonds · protein-protein
H–I · 2719 Å² buried · 13 hydrogen bonds · protein-protein
L–M · 2718 Å² buried · 13 hydrogen bonds · protein-protein
R–S · 2412 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

6VZ8 · Arabidopsis thaliana acetohydroxyacid synthase complex with valine bound · the same entry in another collection · chain K against K, 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 6VZ8 · PDBe 6VZ8 · UniProt P17597 · UniProt Q93YZ7

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