Structure of PDB 6kqj Chain E

Receptor sequence
>6kqjE (length=328) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
DKTVLDANLDPLKGKTIGVIGYGNQGRVQATIMRENGLNVIVGNVKDKYY
ELAKKEGFEVYEIDEAVRRSDVALLLIPDEVMKEVYEKKIAPVLQGKKEF
VLDFASGYNVAFGLIRPPKSVDTIMVAPRMVGEGIMDLHKQGKGYPVLLG
VKQDASGKAWDYAKAIAKGIGAIPGGIAVISSFEEEALLDLMSEHTWVPI
LFGAIKACYDIAVKEYGVSPEAALLEFYASGELAEIARLIAEEGIFNQMV
HHSTTSQYGTLTRMFKYYDVVRRIVENEAKYIWDGSFAKEWSLEQQAGYP
VFYRLWELATQSEMAKAEKELYKLLGRK
3D structure
PDB6kqj Temperature-Resolved Cryo-EM Uncovers Structural Bases of Temperature-Dependent Enzyme Functions.
ChainE
Resolution2.54 Å
3D
structure
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Enzymatic activity
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 E D191 E195 D190 E194
BS02 NAI E N25 Q26 Y50 I78 D80 A106 M131 N24 Q25 Y49 I77 D79 A105 M130
BS03 9TY E D191 E195 D190 E194
BS04 MG E E227 E233 E226 E232
BS05 9TY E E233 S254 E232 S253
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:6kqj, PDBe:6kqj, PDBj:6kqj
PDBsum6kqj
PubMed31829582
UniProtQ97YJ9|ILVC2_SACS2 Putative ketol-acid reductoisomerase 2 (Gene Name=ilvC2)

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