Structure of PDB 6jcz Chain E

Receptor sequence
>6jczE (length=329) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence]
KTVLDANLDPLKGKTIGVIGYGNQGRVQATIMRENGLNVIVGNVKDKYYE
LAKKEGFEVYEIDEAVRRSDVALLLIPDEVMKEVYEKKIAPVLQGKKEFV
LDFASGYNVAFGLIRPPKSVDTIMVAPRMVGEGIMDLHKQGKGYPVLLGV
KQDASGKAWDYAKAIAKGIGAIPGGIAVISSFEEEALLDLMSEHTWVPIL
FGAIKACYDIAVKEYGVSPEAALLEFYASGELAEIARLIAEEGIFNQMVH
HSTTSQYGTLTRMFKYYDVVRRIVENEAKYIWDGSFAKEWSLEQQAGYPV
FYRLWELATQSEMAKAEKELYKLLGRKVK
3D structure
PDB6jcz Use of Cryo-EM To Uncover Structural Bases of pH Effect and Cofactor Bispecificity of Ketol-Acid Reductoisomerase.
ChainE
Resolution3.35 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D189 E193
BS02 NDP E Y23 G24 Q26 N45 V46 Y50 V82 Y21 G22 Q24 N43 V44 Y48 V80
BS03 9TY E D191 E195 D189 E193
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6jcz, PDBe:6jcz, PDBj:6jcz
PDBsum6jcz
PubMed30921515
UniProtQ97YJ9|ILVC2_SACS2 Putative ketol-acid reductoisomerase 2 (Gene Name=ilvC2)

[Back to BioLiP]