Structure of PDB 3pbk Chain B

Receptor sequence
>3pbkB (length=550) Species: 217992 (Escherichia coli O6) [Search protein sequence]
LPMRYADFPTLVDALDYAALSSAGMNFYDRRCQLEDQLEYQTLKARAEAG
AKRLLSLNLKKGDRVALIAETSSEFVEAFFACQYAGLVAVPLAIPSWSAK
LQGLLASCQPAAIITGDEWLPLVNAATHDNPELHVLSHAWFKALPEADVA
LQRPVPNDIAYLQYTSGSTRFPRGVIITHREVMANLRAISHDGIKLRPGD
RCVSWLPFYHDMGLVGFLLTPVATQLSVDYLRTQDFAMRPLQWLKLISKN
RGTVSVAPPFGYELCQRRVNEKDLAELDLSCWRVAGIGAEPISAEQLHQF
AECFRQVNFDNKTFMPCYGLAENALAVSFSDEASGVVVNEVDRDILEYQG
KAVAPGAETRAVSTFVNCGKALPEHGIEIRNEAGMPVAERVVGHICISGP
SLMSGYFGDQVSQDEIAATGWLDTGDLGYLLDGYLYVTGRIKDLIIIRGR
NIWPQDIEYIAEQEPEIHSGDAIAFVTAQEKIILQIQCRISDEERRGQLI
HALAARIQSEFGVTAAIDLLPPHSIPRTSSGKPARAEAKKRYQKAYAASL
3D structure
PDB3pbk Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.
ChainB
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T184 N204 H229 A340 E341 I465 N470 K551
Catalytic site (residue number reindexed from 1) T165 N185 H210 A321 E322 I446 N451 K532
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 B F236 A308 E309 P310 C336 Y337 G338 L339 A340 L344 D445 V456 R459 K551 F217 A289 E290 P291 C317 Y318 G319 L320 A321 L325 D426 V437 R440 K532
Gene Ontology
Molecular Function
GO:0016877 ligase activity, forming carbon-sulfur bonds
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:3pbk, PDBe:3pbk, PDBj:3pbk
PDBsum3pbk
PubMed21185305
UniProtA0A0H2VDD9

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