Structure of PDB 4xdy Chain A

Receptor sequence
>4xdyA (length=331) Species: 285389 (uncultured archaeon GZfos26G2) [Search protein sequence]
MEILHDEDVDDSILRDKTIAVMGYGAQGDAQANCLKDSGINVVIGETEIL
GGNKNPSWEKAKEDGFEVLPIDKAAEKGDVVHILLPDEVQPAIYENQIKP
QLKAGKALCFSHGFNICFKRIVPPEDVDVIMVAPKAPGTEERKAYLEGFG
VPGLVAVKQNPSGEAREVALAMTKAMHWTKAGILECTFEQETYEDLFGEQ
CVLCGGLVELMRNGFEVLVEAGYPPEMAYFECVHEMKLIVDLVWQGGIKR
MAEVISNTAEYGMWAVGHQIIGPEVKEKMKEALKRVENGEFANEWVDEYK
RGIPFLKASREKMGEHQVETVGAEIRKLFAQ
3D structure
PDB4xdy Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases.
ChainA
Resolution1.535 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K135 D195 E199
Catalytic site (residue number reindexed from 1) K135 D195 E199
Enzyme Commision number 1.1.1.382: ketol-acid reductoisomerase (NAD(+)).
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 A D195 E199 D195 E199
BS02 NAI A G25 A26 Q27 E46 L50 N55 S57 L84 L85 P86 D87 I93 H112 P137 G25 A26 Q27 E46 L50 N55 S57 L84 L85 P86 D87 I93 H112 P137
BS03 HIO A P137 D195 E199 P137 D195 E199
BS04 HIO A E235 I239 I255 S256 A259 E235 I239 I255 S256 A259
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:4xdy, PDBe:4xdy, PDBj:4xdy
PDBsum4xdy
PubMed25849365
UniProtQ64BR7|ILVC_UNCAG Ketol-acid reductoisomerase (NAD(+)) (Gene Name=ilvC)

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