Structure of PDB 5etr Chain A

Receptor sequence
>5etrA (length=157) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
MIQAYLGLGSNIGDRESQLNDAIKILNEYDGISVSNISPIYETAPVGYTE
QPNFLNLCVEIQTTLTVLQLLECCLKTEECLHRIRKERWGPRTLDVDILL
YGEEMIDLPKLSVPHPRMNERAFVLIPLNDIAANVVEPRSKLKVKDLVFV
DDSVKRY
3D structure
PDB5etr Structural Basis for the Selective Binding of Inhibitors to 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase from Staphylococcus aureus and Escherichia coli.
ChainA
Resolution1.32 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) R83 R92 D95 D97
Catalytic site (residue number reindexed from 1) R83 R92 D95 D97
Enzyme Commision number 2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
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 APC A L71 R83 D95 D97 I98 K110 L111 S112 H115 R117 R121 L71 R83 D95 D97 I98 K110 L111 S112 H115 R117 R121
BS02 5RW A T43 A44 V46 Y48 Q51 F54 N56 G90 R92 F123 T43 A44 V46 Y48 Q51 F54 N56 G90 R92 F123 MOAD: Kd=0.3uM
BS03 MG A D95 D97 D95 D97
BS04 MG A D95 D97 D95 D97
Gene Ontology
Molecular Function
GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0016310 phosphorylation
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5etr, PDBe:5etr, PDBj:5etr
PDBsum5etr
PubMed27094768
UniProtQ2G0Q5

[Back to BioLiP]