Structure of PDB 3x1j Chain A

Receptor sequence
>3x1jA (length=158) Species: 350703 (Pseudomonas aeruginosa 2192) [Search protein sequence]
MNRVLYPGTFDPITKGHGDLIERASRLFDHVIIAVAASPKKNPLFSLEQR
VALAQEVTKHLPNVEVVGFSTLLAHFVKEQKANVFLRGLRAVSDFEYEFQ
LANMNRQLAPDVESMFLTPSEKYSFISSTLVREIAALGGDISKFVHPAVA
DALAERFK
3D structure
PDB3x1j Transition of phosphopantetheine adenylyltransferase from catalytic to allosteric state is characterized by ternary complex formation in Pseudomonas aeruginosa
ChainA
Resolution2.334 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) 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 ACO A Y6 P7 G8 T9 H17 A36 K41 F69 L72 L73 R87 G88 R90 L101 N105 S127 S128 T129 Y6 P7 G8 T9 H17 A36 K41 F69 L72 L73 R87 G88 R90 L101 N105 S127 S128 T129 MOAD: Ki=8.4uM
BS02 ACO A I134 L137 I134 L137 MOAD: Ki=8.4uM
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:3x1j, PDBe:3x1j, PDBj:3x1j
PDBsum3x1j
PubMed27041211
UniProtA0A0X1KGP2

[Back to BioLiP]