Structure of PDB 4bku Chain A Binding Site BS02

Receptor Information

>4bku Chain A (length=257) Species: 884204 (Burkholderia pseudomallei 1026b)

GFLDGKRILLTGLLSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITEF
AAEFGSELVFPCDVADDAQIDALFASLKTHWDSLDGLVHSIGFAPREAIA
GDFLDGLTRENFRIAHDISAYSFPALAKAALPMLSDDASLLTLSYLGAER
AIPNYNTMGLAKAALEASVRYLAVSLGAKGVRVNAISAGPIKTLAASGIK
SFGKILDFVESNSPLKRNVTIEQVGNAGAFLLSDLASGVTAEVMHVDSGF
NAVVGGM

Ligand information

• Ligand ID: 1S5
• InChI: InChI=1S/C19H26N2O2/c1-4-5-6-7-8-16-12-17(22)19(13-21(16)3)23-18-10-9-15(20)11-14(18)2/h9-13H,4-8,20H2,1-3H3/p+1
• InChIKey: YALGUPBMXZEXMF-UHFFFAOYSA-O
• SMILES:
  ACDLabs 12.01: O(c1c[n+](c(cc1O)CCCCCC)C)c2ccc(N)cc2C
  CACTVS 3.370: CCCCCCC1=CC(=O)C(=CN1C)Oc2ccc(N)cc2C
  OpenEye OEToolkits 1.7.6: CCCCCCC1=CC(=O)C(=CN1C)Oc2ccc(cc2C)N
• Formula: C19 H26 N2 O2
• Name: 5-(4-amino-2-methylphenoxy)-2-hexyl-4-hydroxy-1-methylpyridinium
• PDB chain: 4bku Chain A Residue 1260

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4bku Rational Design of Broad Spectrum Antibacterial Activity Based on a Clinically Relevant Enoyl-Acyl Carrier Protein (Acp) Reductase Inhibitor.
• Resolution: 1.841 Å
• Binding residue (original residue number in PDB): G93 A95 I100 Y146 P154 N155 Y156 M159 F203 I206
• Binding residue (residue number reindexed from 1): G92 A94 I99 Y145 P153 N154 Y155 M158 F202 I205
• Annotation score: 1

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).

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

External links

• PDB: RCSB:4bku, PDBe:4bku, PDBj:4bku
• PDBsum: 4bku
• PubMed: 24739388
• UniProt: A0A0H3HP34