Structure of PDB 5etp Chain A

Receptor sequence

>5etpA (length=160) Species: 562 (Escherichia coli)

AMTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQ
DQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDI
MLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILH
TRAFDKLNKW

3D structure

• PDB: 5etp Structural Basis for the Selective Binding of Inhibitors to 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase from Staphylococcus aureus and Escherichia coli.
• Chain: A
• Resolution: 1.05 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R82 R92 D95 D97
• Catalytic site (residue number reindexed from 1): R84 R94 D97 D99
• 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	Q74 R82 R84 W89 R92 D95 D97 I98 R110 L111 T112 H115 Y116 R121	Q76 R84 R86 W91 R94 D97 D99 I100 R112 L113 T114 H117 Y118 R123
BS02	CA	A	G26 I28 S31	G28 I30 S33
BS03	CA	A	D49 E87	D51 E89
BS04	CA	A	D95 D97	D97 D99
BS05	CA	A	D95 D97	D97 D99
BS06	5RZ	A	T42 P43 L45 Y53 N55 W89 R121 F123	T44 P45 L47 Y55 N57 W91 R123 F125	MOAD: Kd=0.7uM PDBbind-CN: -logKd/Ki=6.15,Kd=0.7uM BindingDB: Kd=700nM

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity

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:5etp, PDBe:5etp, PDBj:5etp
• PDBsum: 5etp
• PubMed: 27094768
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)