Structure of PDB 5etv Chain A

Receptor sequence

>5etvA (length=158) Species: 1280 (Staphylococcus aureus)

HMIQAYLGLGSNIGDRESQLNDAIKILNEYDGISVSNISPIYETAPVGYT
EQPNFLNLCVEIQTTLTVLQLLECCLKTEECLHRIRKERWGPRTLDVDIL
LYGEEMIDLPKLSVPHPRMNERAFVLIPLNDIAANVVEPRSKLKVKDLVF
VDDSVKRY

3D structure

• PDB: 5etv Structural Basis for the Selective Binding of Inhibitors to 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase from Staphylococcus aureus and Escherichia coli.
• Chain: A
• Resolution: 1.72 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R83 R92 D95 D97
• Catalytic site (residue number reindexed from 1): R84 R93 D96 D98
• 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 R92 D95 D97 I98 K110 L111 S112 H115 R121	L72 R84 R93 D96 D98 I99 K111 L112 S113 H116 R122
BS02	5RZ	A	T43 A44 P45 V46 G47 F54 N56 R121 F123	T44 A45 P46 V47 G48 F55 N57 R122 F124	MOAD: Kd=0.57uM PDBbind-CN: -logKd/Ki=6.24,Kd=0.57uM
BS03	MG	A	D95 D97	D96 D98
BS04	MG	A	D95 D97	D96 D98

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:5etv, PDBe:5etv, PDBj:5etv
• PDBsum: 5etv
• PubMed: 27094768
• UniProt: Q2G0Q5