Structure of PDB 4f7v Chain A

Receptor sequence

>4f7vA (length=158) Species: 83333 (Escherichia coli K-12)

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIML
FGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTR
AFDKLNKW

3D structure

• PDB: 4f7v Bisubstrate analog inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: New lead exhibits a distinct binding mode.
• Chain: A
• Resolution: 1.73 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	J1D	A	T42 L45 Y53 N55 L70 Q74 E77 W89 R92 D95 L96 D97 I98 R110 L111 T112 Y116 F123	T42 L45 Y53 N55 L70 Q74 E77 W89 R92 D95 L96 D97 I98 R110 L111 T112 Y116 F123	MOAD: Kd=4.16uM PDBbind-CN: -logKd/Ki=5.38,Kd=4.16uM BindingDB: IC50=9530nM,Kd=4160nM

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:4f7v, PDBe:4f7v, PDBj:4f7v
• PDBsum: 4f7v
• PubMed: 22727779
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)