Structure of PDB 4xdz Chain B

Receptor sequence
>4xdzB (length=329) Species: 583356 (Ignisphaera aggregans DSM 17230) [Search protein sequence]
AKIYKDEDISLEPIKNKTIAILGYGSQGRAWALNLRDSGLNVVVGLERQG
DSWRRAIDDGFKPMYTKDAVAIADIIVFLVPDMVQKSLWLNSVKDFMKKG
ADLVFAHGFNIHFKIIEPPKDSDVYMIAPKSPGPIVRRSYEMGGGVPALV
AVYQNVSGEALQKALAIAKGIGCARAGVIESTFKEETETDLFGEQVILVG
GIMELIKASFETLVEEGYQPEVAYFETVNELKLIVDLIYEKGLTGMLRAV
SDTAKYGGITVGKFIIDKSVRDKMKIVLERIRSGEFAREWIKEYERGMPT
VFKELSELEGSTIETVGRKLREMMFRGMK
3D structure
PDB4xdz Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases.
ChainB
Resolution1.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K131 D191 E195
Catalytic site (residue number reindexed from 1) K130 D190 E194
Enzyme Commision number 1.1.1.383: ketol-acid reductoisomerase [NAD(P)(+)].
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 40E B E231 V251 S252 A255 E230 V250 S251 A254
BS02 NDP B Y25 G26 S27 Q28 E48 R49 S53 L80 V81 P82 D83 V85 A107 H108 P133 Y24 G25 S26 Q27 E47 R48 S52 L79 V80 P81 D82 V84 A106 H107 P132
BS03 MG B D191 E195 D190 E194
BS04 40E B P133 D191 E195 P132 D190 E194
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004455 ketol-acid reductoisomerase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050661 NADP 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

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Molecular Function

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Biological Process
External links
PDB RCSB:4xdz, PDBe:4xdz, PDBj:4xdz
PDBsum4xdz
PubMed25849365
UniProtE0SRA9|ILVC_IGNAA Ketol-acid reductoisomerase (NAD(P)(+)) (Gene Name=ilvC)

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