Structure of PDB 3sj7 Chain A

Receptor sequence
>3sj7A (length=239) Species: 93061 (Staphylococcus aureus subsp. aureus NCTC 8325) [Search protein sequence]
TKSALVTGASRGIGRSIALQLAEEGYNVAVNYAGSKEKAEAVVEEIKAKG
VDSFAIQANVADADEVKAMIKEVVSQFGSLDVLVNNAGITRDNLLMRMKE
QEWDDVIDTNLKGVFNCIQKATPQMLRQRSGAIINLSSVVGAVGNPGQAN
YVATKAGVIGLTKSAARELASRGITVNAVAPGFIVSDMTDELKEQMLTQI
PLARFGQDTDIANTVAFLASDKAKYITGQTIHVNGGMYM
3D structure
PDB3sj7 Crystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal fabg1 in positive cooperativity for NADPH.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G13 S139 Q149 Y152 K156
Catalytic site (residue number reindexed from 1) G12 S138 Q148 Y151 K155
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase.
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 NDP A G9 S11 R12 I14 N32 Y33 A34 G35 S36 A59 N60 V61 N87 A88 T110 S139 Y152 K156 P182 G183 G8 S10 R11 I13 N31 Y32 A33 G34 S35 A58 N59 V60 N86 A87 T109 S138 Y151 K155 P181 G182 MOAD: Kd=53.93uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0030497 fatty acid elongation

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Molecular Function
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Biological Process
External links
PDB RCSB:3sj7, PDBe:3sj7, PDBj:3sj7
PDBsum3sj7
PubMed22275129
UniProtQ2FZ53

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