Structure of PDB 3x1k Chain E

Receptor sequence
>3x1kE (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
ChainE
Resolution2.547 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 E Y6 T9 F10 G16 H17 L20 R87 G88 R90 P119 S128 T129 Y5 T8 F9 G15 H16 L19 R86 G87 R89 P118 S127 T128 PDBbind-CN: -logKd/Ki=3.59,Kd=256uM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3x1k, PDBe:3x1k, PDBj:3x1k
PDBsum3x1k
PubMed27041211
UniProtA0A0X1KGP2

[Back to BioLiP]