Structure of PDB 4bku Chain A

Receptor sequence
>4bkuA (length=257) Species: 884204 (Burkholderia pseudomallei 1026b) [Search protein sequence]
GFLDGKRILLTGLLSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITEF
AAEFGSELVFPCDVADDAQIDALFASLKTHWDSLDGLVHSIGFAPREAIA
GDFLDGLTRENFRIAHDISAYSFPALAKAALPMLSDDASLLTLSYLGAER
AIPNYNTMGLAKAALEASVRYLAVSLGAKGVRVNAISAGPIKTLAASGIK
SFGKILDFVESNSPLKRNVTIEQVGNAGAFLLSDLASGVTAEVMHVDSGF
NAVVGGM
3D structure
PDB4bku Rational Design of Broad Spectrum Antibacterial Activity Based on a Clinically Relevant Enoyl-Acyl Carrier Protein (Acp) Reductase Inhibitor.
ChainA
Resolution1.841 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y156 K163
Catalytic site (residue number reindexed from 1) Y155 K162
Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).
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 A G13 S19 I20 D64 V65 S91 I92 G93 L144 S145 K163 A189 P191 G12 S18 I19 D63 V64 S90 I91 G92 L143 S144 K162 A188 P190
BS02 1S5 A G93 A95 I100 Y146 P154 N155 Y156 M159 F203 I206 G92 A94 I99 Y145 P153 N154 Y155 M158 F202 I205
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006633 fatty acid biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4bku, PDBe:4bku, PDBj:4bku
PDBsum4bku
PubMed24739388
UniProtA0A0H3HP34

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