Structure of PDB 3x1k Chain A

Receptor sequence
>3x1kA (length=157) Species: 350703 (Pseudomonas aeruginosa 2192) [Search protein sequence]
NRVLYPGTFDPITKGHGDLIERASRLFDHVIIAVAASPKKNPLFSLEQRV
ALAQEVTKHLPNVEVVGFSTLLAHFVKEQKANVFLRGLRAVSDFEYEFQL
ANMNRQLAPDVESMFLTPSEKYSFISSTLVREIAALGGDISKFVHPAVAD
ALAERFK
3D structure
PDB3x1k Transition of phosphopantetheine adenylyltransferase from catalytic to allosteric state is characterized by ternary complex formation in Pseudomonas aeruginosa
ChainA
Resolution2.547 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H17 K41 R90 S128
Catalytic site (residue number reindexed from 1) H16 K40 R89 S127
Enzyme Commision number 2.7.7.3: pantetheine-phosphate adenylyltransferase.
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 ANP A Y6 G8 T9 G16 H17 L20 R87 G88 R90 D94 E98 P119 S127 S128 T129 Y5 G7 T8 G15 H16 L19 R86 G87 R89 D93 E97 P118 S126 S127 T128 PDBbind-CN: -logKd/Ki=3.59,Kd=256uM
BS02 PO4 A P110 E113 P109 E112
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004595 pantetheine-phosphate adenylyltransferase activity
GO:0005524 ATP binding
GO:0008771 [citrate (pro-3S)-lyase] ligase activity
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0015937 coenzyme A biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3x1k, PDBe:3x1k, PDBj:3x1k
PDBsum3x1k
PubMed27041211
UniProtA0A0X1KGP2

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