Structure of PDB 3fr7 Chain B

Receptor sequence

>3fr7B (length=490) Species: 39947 (Oryza sativa Japonica Group)

LDFDTSVFNKEKVSLAGHEEYIVRGGRNLFPLLPEAFKGIKQIGVIGWGS
QGPAQAQNLRDSLAEAKSDIVVKIGLRKGSKSFDEARAAGFTEESGTLGD
IWETVSGSDLVLLLISDAAQADNYEKIFSHMKPNSILGLSHGFLLGHLQS
AGLDFPKNISVIAVCPKGMGPSVRRLYVQGKEINGAGINSSFAVHQDVDG
RATDVALGWSVALGSPFTFATTLEQEYKSDIFGERGILLGAVHGIVEALF
RRYTEQGMDEEMAYKNTVEGITGIISKTISKKGMLEVYNSLTEEGKKEFN
KAYSASFYPCMDILYECYEDVASGSEIRSVVLAGRRFYEKEGLPAFPMGN
IDQTRMWKVGEKVRSTRPENDLGPLHPFTAGVYVALMMAQIEVLRKKGHS
YSEIINESVIESVDSLNPFMHARGVAFMVDNCSTTARLGSRKWAPRFDYI
LTQQAFVTVDKDAPINQDLISNFMSDPVHGAIEVCAELRP

3D structure

• PDB: 3fr7 Conformational changes in a plant ketol-acid reductoisomerase upon Mg(2+) and NADPH binding as revealed by two crystal structures
• Chain: B
• Resolution: 1.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K1252 D1315 E1319
• Catalytic site (residue number reindexed from 1): K167 D230 E234
• 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	B	D1315 E1319	D230 E234

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004455 ketol-acid reductoisomerase activity
• GO:0016491 oxidoreductase activity
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding
• GO:0070402 NADPH 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:0009507 chloroplast

External links

• PDB: RCSB:3fr7, PDBe:3fr7, PDBj:3fr7
• PDBsum: 3fr7
• PubMed: 19362563
• UniProt: Q65XK0|ILV5_ORYSJ Ketol-acid reductoisomerase, chloroplastic (Gene Name=Os05g0573700)