Structure of PDB 6jd2 Chain F Binding Site BS01

Receptor Information
>6jd2 Chain F (length=326) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTVLDANLDPLKGKTIGVIGYGNQGRVQATIMRENGLNVIVGNVKDKYYE
LAKKEGFEVYEIDEAVRRSDVALLLIPDEVMKEVYEKKIAPVLQGKKEFV
LDFASGYNVAFGLIRPPKSVDTIMVAPRMVGEGIMDLHKQGKGYPVLLGV
KQDASGKAWDYAKAIAKGIGAIPGGIAVISSFEEEALLDLMSEHTWVPIL
FGAIKACYDIAVKEYGVSPEAALLEFYASGELAEIARLIAEEGIFNQMVH
HSTTSQYGTLTRMFKYYDVVRRIVENEAKYIWDGSFAKEWSLEQQAGYPV
FYRLWELATQSEMAKAEKELYKLLGR
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain6jd2 Chain F Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6jd2 Use of Cryo-EM To Uncover Structural Bases of pH Effect and Cofactor Bispecificity of Ketol-Acid Reductoisomerase.
Resolution2.53 Å
Binding residue
(original residue number in PDB)		E227 E233
Binding residue
(residue number reindexed from 1)		E225 E231
Annotation score1
Enzymatic activity
Enzyme Commision number 1.1.1.86: ketol-acid reductoisomerase (NADP(+)).
Gene Ontology
Molecular Function
GO:0004455 ketol-acid reductoisomerase activity
GO:0016491 oxidoreductase activity
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6jd2, PDBe:6jd2, PDBj:6jd2
PDBsum6jd2
PubMed30921515
UniProtQ97YJ9|ILVC2_SACS2 Putative ketol-acid reductoisomerase 2 (Gene Name=ilvC2)

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