Structure of PDB 4bni Chain B

Receptor sequence

>4bniB (length=255) Species: 158879 (Staphylococcus aureus subsp. aureus N315)

VNLENKTYVIMGIANKRSIAFGVAKVLDQLGAKLVFTYRKERSRKELEKL
LEQLNQPEAHLYQIDVQSDEEVINGFEQIGKDVGNIDGVYHSIAFANMED
LRGRFSETSREGFLLAQDISSYSLTIVAHEAKKLMPEGGSIVATTYLGGE
FAVQNYNVMGVAKASLEANVKYLALDLGPDNIRVNAISAGPIRTLSAKGV
GGFNTILKEIEERAPLKRNVDQVEVGKTAAYLLSDLSSGVTGENIHVDSG
FHAIK

3D structure

• PDB: 4bni Rational Optimization of Drug-Target Residence Time: Insights from Inhibitor Binding to the S. Aureus Fabi Enzyme-Product Complex.
• Chain: B
• Resolution: 2.2 Å

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	B	K7 D88 G140 R184 D236	K6 D87 G139 R183 D235
BS02	P1F	B	A95 Y147 Y157 M160 S197 A198 V201	A94 Y146 Y156 M159 S196 A197 V200	MOAD: Ki=120pM
BS03	NAP	B	G13 A15 S19 I20 R40 K41 S44 D66 V67 S93 I94 A95 I120 T145 T146 Y147 K164 A190 P192 I193 T195 S197	G12 A14 S18 I19 R39 K40 S43 D65 V66 S92 I93 A94 I119 T144 T145 Y146 K163 A189 P191 I192 T194 S196

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

External links

• PDB: RCSB:4bni, PDBe:4bni, PDBj:4bni
• PDBsum: 4bni
• PubMed: 23697754
• UniProt: A0A0H3JLH9