Structure of PDB 3lnv Chain A

Receptor sequence
>3lnvA (length=566) Species: 272624 (Legionella pneumophila subsp. pneumophila str. Philadelphia 1) [Search protein sequence]
SLKKEYLQCQSLVDVVRLRALHSPNKKSCTFLNKELEETMTYEQLDQHAK
AIAATLQAEGAKPGDRVLLLFAPGLPLIQAFLGCLYAGCIAVPIYPPAQE
KLLDKAQRIVTNSKPVIVLMIADHIKKFTPKFLKIPAIALESIELNRSSS
WQPTSIKSNDIAFLQYTSGSTMHPKGVMVSHHNLLDNLNKIFTSFHMNDE
TIIFSWLPPHHDMGLIGCILTPIYGGIQAIMMSPFSFLQNPLSWLKHITK
YKATISGSPNFAYDYCVKRIREEKKEGLDLSSWVTAFNGAEPVREETMEH
FYQAFKEFGFRKEAFYPCYGLAEATLLVTGGTPGSSYKTLTLAKEQFQDH
RVHFADDSPGSYKLVSSGNPIQEVKIIDPDTLIPCDFDQVGEIWVQSNSV
AKGYWNQPEETRHAFAGKIKDDSAIYLRTGDLGFLHENELYVTGRIKDLI
IIYGKNHYPQDIEFSLMHSPLHHVLGKCAAFVIQEEHEYKLTVMCEVKNR
FMDDVAQDNLFNEIFELVYENHQLEVHTIVLIPLKAMPHSGKIRRNFCRK
HLLDLPIVATWQLNKI
3D structure
PDB3lnv Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N193 H217 A328 I460 K553
Catalytic site (residue number reindexed from 1) N187 H211 A322 I451 K542
Enzyme Commision number ?
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 S174 F201 M219 G223 F293 A296 E297 P298 C324 Y325 G326 L327 L332 D440 R454 S168 F195 M213 G217 F287 A290 E291 P292 C318 Y319 G320 L321 L326 D431 R445
BS02 POP A T173 G175 S176 E329 T167 G169 S170 E323
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3lnv, PDBe:3lnv, PDBj:3lnv
PDBsum3lnv
PubMed21185305
UniProtQ5ZTD3

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