Structure of PDB 6kph Chain G

Receptor sequence
>6kphG (length=328) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
DKTVLDANLDPLKGKTIGVIGYGNQGRVQATIMRENGLNVIVGNVKDKYY
ELAKKEGFEVYEIDEAVRRSDVALLLIPDEVMKEVYEKKIAPVLQGKKEF
VLDFASGYNVAFGLIRPPKSVDTIMVAPRMVGEGIMDLHKQGKGYPVLLG
VKQDASGKAWDYAKAIAKGIGAIPGGIAVISSFEEEALLDLMSEHTWVPI
LFGAIKACYDIAVKEYGVSPEAALLEFYASGELAEIARLIAEEGIFNQMV
HHSTTSQYGTLTRMFKYYDVVRRIVENEAKYIWDGSFAKEWSLEQQAGYP
VFYRLWELATQSEMAKAEKELYKLLGRK
3D structure
PDB6kph Temperature-Resolved Cryo-EM Uncovers Structural Bases of Temperature-Dependent Enzyme Functions.
ChainG
Resolution2.41 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 G D191 E195 D190 E194
BS02 NAI G Y23 N25 Q26 N45 Y50 P79 D80 V82 A106 S107 M131 V132 Y22 N24 Q25 N44 Y49 P78 D79 V81 A105 S106 M130 V131
BS03 9TY G D191 E195 D190 E194
BS04 9TY G E233 H253 S254 S257 E232 H252 S253 S256
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:6kph, PDBe:6kph, PDBj:6kph
PDBsum6kph
PubMed31829582
UniProtQ97YJ9|ILVC2_SACS2 Putative ketol-acid reductoisomerase 2 (Gene Name=ilvC2)

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