Structure of PDB 5etl Chain A

Receptor sequence

>5etlA (length=155) Species: 562 (Escherichia coli)

SAMTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGP
QDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKRTLDLDIMLFGN
EVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFD
KLNKW

3D structure

• PDB: 5etl Structural Basis for the Selective Binding of Inhibitors to 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase from Staphylococcus aureus and Escherichia coli.
• Chain: A
• Resolution: 1.82 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R82 R92 D95 D97
• Catalytic site (residue number reindexed from 1): R85 R89 D92 D94
• 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	CA	A	D95 D97	D92 D94
BS02	CA	A	D95 D97	D92 D94
BS03	CA	A	K119 P138 D139	K116 P135 D136
BS04	ATP	A	L70 Q74 R82 R84 R92 D95 D97 I98 R110 L111 T112 H115 Y116 R121	L73 Q77 R85 R87 R89 D92 D94 I95 R107 L108 T109 H112 Y113 R118
BS05	5RV	A	T42 P43 L45 Y53 N55 R121 F123	T45 P46 L48 Y56 N58 R118 F120	MOAD: Kd=23uM PDBbind-CN: -logKd/Ki=4.64,Kd=23uM

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