Structure of PDB 1yve Chain L

Receptor sequence

>1yveL (length=513) Species: 3562 (Spinacia oleracea)

ATTFDFDSSVFKKEKVTLSGHDEYIVRGGRNLFPLLPDAFKGIKQIGVIG
WGSQAPAQAQNLKDSLTEAKSDVVVKIGLRKGSNSFAEARAAGFSEENGT
LGDMWETISGSDLVLLLISDSAQADNYEKVFSHMKPNSILGLSHGFLLGH
LQSLGQDFPKNISVIAVCPKGMGPSVRRLYVQGKEVNGAGINSSFAVHQD
VDGRATDVALGWSIALGSPFTFATTLEQEYKSDIFGERGILLGAVHGIVE
CLFRRYTESGMSEDLAYKNTVECITGVISKTISTKGMLALYNSLSEEGKK
DFQAAYSASYYPSMDILYECYEDVASGSEIRSVVLAGRRFYEKEGLPAFP
MGKIDQTRMWKVGEKVRSVRPAGDLGPLYPFTAGVYVALMMAQIEILRKK
GHSYSEIINESVIEAVDSLNPFMHARGVSFMVDNCSTTARLGSRKWAPRF
DYILSQQALVAVDNGAPINQDLISNFLSDPVHEAIGVCAQLRPSVDISVT
ADADFVRPELRQA

3D structure

• PDB: 1yve The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution.
• Chain: L
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K252 D315 E319
• Catalytic site (residue number reindexed from 1): K170 D233 E237
• Enzyme Commision number: 1.1.1.86: ketol-acid reductoisomerase (NADP(+)).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	NDP	L	G132 W133 S135 Q136 R162 S165 S167 L199 I200 S201 D202 A204 H226 M254 S518 T519 R589	G50 W51 S53 Q54 R80 S83 S85 L117 I118 S119 D120 A122 H144 M172 S436 T437 R507
BS02	MG	L	D315 E319	D233 E237
BS03	HIO	L	M254 D315 E319 E496 L501 C517 S518 A521	M172 D233 E237 E414 L419 C435 S436 A439

Gene Ontology

Molecular Function

• GO:0004455 ketol-acid reductoisomerase activity
• GO:0016491 oxidoreductase activity

Biological Process

• GO:0009082 branched-chain amino acid biosynthetic process

External links

• PDB: RCSB:1yve, PDBe:1yve, PDBj:1yve
• PDBsum: 1yve
• PubMed: 9218783
• UniProt: Q01292|ILV5_SPIOL Ketol-acid reductoisomerase, chloroplastic (Gene Name=AHRI)