Structure of PDB 7pcl Chain A

Receptor sequence
>7pclA (length=340) Species: 271848 (Burkholderia thailandensis E264) [Search protein sequence]
NDLIYQDEHASLQPLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDD
RYFELARAEGHRVTNIAEAVAHADIVLLLIPDEAHGAVFDVDIAPNLRDG
ALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYF
DIVADHTGRARDRVLAIARAVGFTRAGVMALGYRQETFLDLFQEQFLAPA
LVDLVETGFQVLVERGFNPKAALLEVYGSGEMGKMMLDGADIGLDEVVAL
QGSPTCQVGYHRWRGRTLPTAVRELAARVLDQIEGGDFSAYLKEQASNDY
ASLDDARRAALKRPLNVAHAQVRAAFRFPTEAAGGLYQAA
3D structure
PDB7pcl Pathogenic bacteria remodel central metabolic enzyme to build a cyclopropanol warhead.
ChainA
Resolution2.05 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 NAD A G25 G27 I28 Q29 N48 I49 D51 Y53 I81 P82 D83 A85 V89 A107 H108 Y133 G24 G26 I27 Q28 N47 I48 D50 Y52 I80 P81 D82 A84 V88 A106 H107 Y132
BS02 MG A D191 E195 D190 E194
BS03 76I A D191 E195 D190 E194
BS04 76I A E232 G253 S254 C257 E231 G252 S253 C256
BS05 NAD A Q252 S254 Q251 S253
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004455 ketol-acid reductoisomerase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion 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
View graph for
Biological Process
External links
PDB RCSB:7pcl, PDBe:7pcl, PDBj:7pcl
PDBsum7pcl
PubMed35906404
UniProtQ2T3G7

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