Structure of PDB 5etq Chain A

Receptor sequence

>5etqA (length=157) Species: 1280 (Staphylococcus aureus)

MIQAYLGLGSNIGDRESQLNDAIKILNEYDGISVSNISPIYETAPVGYTE
QPNFLNLCVEIQTTLTVLQLLECCLKTEECLHRIRKERWGPRTLDVDILL
YGEEMIDLPKLSVPHPRMNERAFVLIPLNDIAANVVEPRSKLKVKDLVFV
DDSVKRY

3D structure

• PDB: 5etq Structural Basis for the Selective Binding of Inhibitors to 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase from Staphylococcus aureus and Escherichia coli.
• Chain: A
• Resolution: 1.96 Å

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	MG	A	D95 D97	D95 D97
BS02	MG	A	D95 D97	D95 D97
BS03	APC	A	L71 R83 R85 D95 D97 I98 K110 L111 S112 H115 R117 R121	L71 R83 R85 D95 D97 I98 K110 L111 S112 H115 R117 R121
BS04	YH2	A	T43 A44 P45 V46 Q51 F54 N56 G90 P91 R92 F123	T43 A44 P45 V46 Q51 F54 N56 G90 P91 R92 F123	MOAD: Kd=0.33uM PDBbind-CN: -logKd/Ki=6.48,Kd=0.33uM

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

External links

• PDB: RCSB:5etq, PDBe:5etq, PDBj:5etq
• PDBsum: 5etq
• PubMed: 27094768
• UniProt: Q2G0Q5