Structure of PDB 4bnh Chain F

Receptor sequence
>4bnhF (length=255) Species: 158879 (Staphylococcus aureus subsp. aureus N315) [Search protein sequence]
VNLENKTYVIMGIANKRSIAFGVAKVLDQLGAKLVFTYRKERSRKELEKL
LEQLNQPEAHLYQIDVQSDEEVINGFEQIGKDVGNIDGVYHSIAFANMED
LRGRFSETSREGFLLAQDISSYSLTIVAHEAKKLMPEGGSIVATTYLGGE
FAVQNYNVMGVAKASLEANVKYLALDLGPDNIRVNAISAGPIRTLSAKGV
GGFNTILKEIEERAPLKRNVDQVEVGKTAAYLLSDLSSGVTGENIHVDSG
FHAIK
3D structure
PDB4bnh Rational Optimization of Drug-Target Residence Time: Insights from Inhibitor Binding to the S. Aureus Fabi Enzyme-Product Complex.
ChainF
Resolution2.15 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) Y146 Y156 M159 K163 K198
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 GLU F R103 G203 R102 G202
BS02 NAP F G13 A15 S19 I20 R40 K41 S44 D66 V67 S93 I94 A95 T145 T146 Y147 K164 A190 P192 I193 T195 S197 G12 A14 S18 I19 R39 K40 S43 D65 V66 S92 I93 A94 T144 T145 Y146 K163 A189 P191 I192 T194 S196
BS03 6PN F A95 Y147 Y157 S197 A198 A94 Y146 Y156 S196 A197 MOAD: Ki=10pM
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:4bnh, PDBe:4bnh, PDBj:4bnh
PDBsum4bnh
PubMed23697754
UniProtA0A0H3JLH9

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