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BioLiP

Structure of PDB 4xdy Chain B

Receptor sequence
>4xdyB (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.
ChainB
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 NAI B I255 S256 I255 S256
BS02 HIO B E235 I239 I255 S256 A259 E235 I239 I255 S256 A259
BS03 HIO B P137 D195 E199 P137 D195 E199
BS04 MG B D195 E199 D195 E199
BS05 NAI B 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
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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