Structure of PDB 4all Chain C

Receptor sequence
>4allC (length=254) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
NLENKTYVIMGIANKRSIAFGVAKVLDQLGAKLVFTYRKERSRKELEKLL
EQLNQPEAHLYQIDVQSDEEVINGFEQIGKDVGNIDGVYHSIAFANMEDL
RGRFSETSREGFLLAQDISSYSLTIVAHEAKKLMPEGGSIVATTYLGGEF
AVQNYNVMGVAKASLEANVKYLALDLGPDNIRVNAISAGPIRTLSAKGVG
GFNTILKEIEERAPLKRNVDQVEVGKTAAYLLSDLSSGVTGENIHVDSGF
HAIK
3D structure
PDB4all Staphylococcus Aureus Fabi: Inhibition, Substrate Recognition and Potential Implications for in Vivo Essentiality
ChainC
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y147 Y157 M160 K164 K199
Catalytic site (residue number reindexed from 1) Y145 Y155 M158 K162 K197
Enzyme Commision number 1.3.1.39: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific).
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 NAP C G13 A15 S19 I20 R40 I65 D66 V67 S93 I94 A95 T145 T146 Y147 K164 P192 I193 T195 S197 G11 A13 S17 I18 R38 I63 D64 V65 S91 I92 A93 T143 T144 Y145 K162 P190 I191 T193 S195
BS02 TCL C F96 A97 Y147 Y157 M160 S197 F94 A95 Y145 Y155 M158 S195
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0141148 enoyl-[acyl-carrier-protein] reductase (NADPH) activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4all, PDBe:4all, PDBj:4all
PDBsum4all
PubMed22579249
UniProtA0A0H3JLH9

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