Structure of PDB 4xiy Chain A

Receptor sequence

>4xiyA (length=328) Species: 322710 (Azotobacter vinelandii DJ)

MKVYYDKDCDLSIIQSKKVAIIGYGSQGHAHACNLKDSGVDVYVGLRAGS
ASVAKAEAHGLTVKSVKDAVAAADVVMILTPDEFQGRLYKDEIEPNLKKG
ATLAFAHGFSIHYNQVVPRADLDVIMIAPKAPGHTVRSEFVRGGGIPDLI
AVYQDASGNAKNLALSYACGVGGGRTGIIETTFKDETETDLFGEQAVLCG
GCVELVKAGFETLVEAGYAPEMAYFECLHELKLIVDLMFEGGIANMNYSI
SNNAEYGEYVTGPEVINEQSRQAMRNALKRIQDGEYAKMFITEGAANYPS
MTAYRRNNAAHQIEVVGEKLRTMMPWIA

3D structure

• PDB: 4xiy Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K130 D190 E194
• Catalytic site (residue number reindexed from 1): K130 D190 E194
• 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	MG	A	E226 E230	E226 E230
BS02	FE	A	D190 E194	D190 E194

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004455 ketol-acid reductoisomerase activity
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding
• GO:0050661 NADP binding

Biological Process

• GO:0008652 amino acid biosynthetic process
• GO:0009082 branched-chain amino acid biosynthetic process
• GO:0009097 isoleucine biosynthetic process
• GO:0009099 L-valine biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:4xiy, PDBe:4xiy, PDBj:4xiy
• PDBsum: 4xiy
• PubMed: 25849365
• UniProt: C1DFH7|ILVC_AZOVD Ketol-acid reductoisomerase (NADP(+)) (Gene Name=ilvC)