Structure of PDB 6ccq Chain A

Receptor sequence
>6ccqA (length=156) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERV
ALAQQATAHLGNVEVVGFSDLMANFARNQHATVLIRGLRAVADFEYEMQL
AHMNRHLMPELESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPENVHQ
ALMAKL
3D structure
PDB6ccq Fragment-Based Drug Discovery of Inhibitors of Phosphopantetheine Adenylyltransferase from Gram-Negative Bacteria.
ChainA
Resolution1.92 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) H18 K42 R91 S129
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 EX7 A P8 G9 A37 L73 M74 A75 L102 M105 N106 P6 G7 A35 L71 M72 A73 L100 M103 N104 MOAD: ic50=0.25uM
PDBbind-CN: -logKd/Ki=6.60,IC50=0.25uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004595 pantetheine-phosphate adenylyltransferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0042802 identical protein binding
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:6ccq, PDBe:6ccq, PDBj:6ccq
PDBsum6ccq
PubMed29498517
UniProtP0A6I6|COAD_ECOLI Phosphopantetheine adenylyltransferase (Gene Name=coaD)

[Back to BioLiP]