Structure of PDB 3kxw Chain A

Receptor sequence

>3kxwA (length=572) Species: 272624 (Legionella pneumophila subsp. pneumophila str. Philadelphia 1)

SLKKEYLQCQSLVDVVRLRALHSPNKKSCTFLNKELEETMTYEQLDQHAK
AIAATLQAEGAKPGDRVLLLFAPGLPLIQAFLGCLYAGCIAVPIYPPAQE
KLLDKAQRIVTNSKPVIVLMIADHIKKFTANPKFLKIPAIALESIELNRS
SSWQPTSIKSNDIAFLQYTSGSTMHPKGVMVSHHNLLDNLNKIFTSFHMN
DETIIFSWLPPHHDMGLIGCILTPIYGGIQAIMMSPFSFLQNPLSWLKHI
TKYKATISGSPNFAYDYCVKRIREEKKEGLDLSSWVTAFNGAEPVREETM
EHFYQAFKEFGFRKEAFYPCYGLAEATLLVTGGTPGSSYKTLTLAKEQFQ
DHRVHFADDNSPGSYKLVSSGNPIQEVKIIDPDTLIPCDFDQVGEIWVQS
NSVAKGYWNQPEETRHAFAGKIKDDAIYLRTGDLGFLHENELYVTGRIKD
LIIIYGKNHYPQDIEFSLMHSPLHHVLGKCAAFVIQEEHEYKLTVMCEVK
NRFMDDVAQDNLFNEIFELVYENHQLEVHTIVLIPLKAMPHTTSGKIRRN
FCRKHLLDKTLPIVATWQLNKI

3D structure

• PDB: 3kxw Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.
• Chain: A
• Resolution: 1.851 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N193 H217 A328 I460 K553
• Catalytic site (residue number reindexed from 1): N189 H213 A324 I453 K546

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	1ZZ	A	F201 H217 D218 G223 F293 A296 E297 P298 C324 Y325 G326 L327 A328 L332 D440 V451	F197 H213 D214 G219 F289 A292 E293 P294 C320 Y321 G322 L323 A324 L328 D433 V444

Gene Ontology

Molecular Function

• GO:0070566 adenylyltransferase activity

Biological Process

• GO:0006633 fatty acid biosynthetic process
• GO:0008610 lipid biosynthetic process

Cellular Component

• GO:0005886 plasma membrane

External links

• PDB: RCSB:3kxw, PDBe:3kxw, PDBj:3kxw
• PDBsum: 3kxw
• PubMed: 21185305
• UniProt: Q5ZTD3