Structure of PDB 1ex8 Chain A

Receptor sequence

>1ex8A (length=158) Species: 562 (Escherichia coli)

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIML
FGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTR
AFDKLNKW

3D structure

• PDB: 1ex8 Bisubstrate analogue inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: synthesis and biochemical and crystallographic studies.
• Chain: A
• Resolution: 1.85 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R82 R92 D95 D97
• Catalytic site (residue number reindexed from 1): R82 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	A4P	A	T42 P43 L45 Y53 N55 Q74 R82 R84 R88 W89 R92 D97 I98 R110 L111 T112 H115 F123	T42 P43 L45 Y53 N55 Q74 R82 R84 R88 W89 R92 D97 I98 R110 L111 T112 H115 F123	MOAD: Kd=0.47uM PDBbind-CN: -logKd/Ki=6.33,Kd=0.47uM

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:1ex8, PDBe:1ex8, PDBj:1ex8
• PDBsum: 1ex8
• PubMed: 11311059
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)