Structure of PDB 4ruk Chain E

Receptor sequence
>4rukE (length=158) Species: 350703 (Pseudomonas aeruginosa 2192) [Search protein sequence]
MNRVLYPGTFDPITKGHGDLIERASRLFDHVIIAVAASPKKNPLFSLEQR
VALAQEVTKHLPNVEVVGFSTLLAHFVKEQKANVFLRGLRAVSDFEYEFQ
LANMNRQLAPDVESMFLTPSEKYSFISSTLVREIAALGGDISKFVHPAVA
DALAERFK
3D structure
PDB4ruk Transition of phosphopantetheine adenylyltransferase from catalytic to allosteric state is characterized by ternary complex formation in Pseudomonas aeruginosa
ChainE
Resolution2.2 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) H17 K41 R90 S128
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 COA E E133 L137 E133 L137
BS02 COA E G8 T9 F10 S38 K41 F69 S70 T71 L73 R87 Y97 S127 S128 T129 G8 T9 F10 S38 K41 F69 S70 T71 L73 R87 Y97 S127 S128 T129
BS03 CA E H17 S128 H17 S128
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4ruk, PDBe:4ruk, PDBj:4ruk
PDBsum4ruk
PubMed27041211
UniProtA0A0X1KGP2

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