Structure of PDB 3pbk Chain A

Receptor sequence
>3pbkA (length=555) Species: 217992 (Escherichia coli O6) [Search protein sequence]
PMRYADFPTLVDALDYAALSSAGMNFYDRRCQLEDQLEYQTLKARAEAGA
KRLLSLNLKKGDRVALIAETSSEFVEAFFACQYAGLVAVPLAIPMGVGQR
DSWSAKLQGLLASCQPAAIITGDEWLPLVNAATHDNPELHVLSHAWFKAL
PEADVALQRPVPNDIAYLQYTSGSTRFPRGVIITHREVMANLRAISHDGI
KLRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLRTQDFAMRPLQWL
KLISKNRGTVSVAPPFGYELCQRRVNEKDLAELDLSCWRVAGIGAEPISA
EQLHQFAECFRQVNFDNKTFMPCYGLAENALAVSFSDEASGVVVNEVDRD
ILEYQGKAVAPGAETRAVSTFVNCGKALPEHGIEIRNEAGMPVAERVVGH
ICISGPSLMSGYFGDQVSQDEIAATGWLDTGDLGYLLDGYLYVTGRIKDL
IIIRGRNIWPQDIEYIAEQEPEIHSGDAIAFVTAQEKIILQIQCRISDEE
RRGQLIHALAARIQSEFGVTAAIDLLPPHSIPRTSSGKPARAEAKKRYQK
AYAAS
3D structure
PDB3pbk Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.
ChainA
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) T171 N191 H216 A327 E328 I452 N457 K538
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 D230 G235 A308 E309 P310 C336 Y337 G338 L339 A340 L344 D445 V456 D217 G222 A295 E296 P297 C323 Y324 G325 L326 A327 L331 D432 V443
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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