Structure of PDB 1ru1 Chain A

Receptor sequence

>1ru1A (length=143) Species: 562 (Escherichia coli)

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPPDYLNA
AVALETSLAPEELLNHTQRIELQQGRRTLDLDIMLFGNEVINTERLTVPH
YDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW

3D structure

• PDB: 1ru1 Essential Roles of a Dynamic Loop in the Catalysis of 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase.
• Chain: A
• Resolution: 1.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R92 D95 D97
• Catalytic site (residue number reindexed from 1): R77 D80 D82
• 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	MG	A	D95 D97	D80 D82
BS02	MG	A	D95 D97	D80 D82
BS03	APC	A	Q74 D95 D97 I98 R110 L111 T112 H115 Y116 R121	Q68 D80 D82 I83 R95 L96 T97 H100 Y101 R106	PDBbind-CN: -logKd/Ki=4.74,Kd=18uM
BS04	PH2	A	T42 P43 Y53 N55 D95 F123	T42 P43 Y47 N49 D80 F108	MOAD: Kd=18uM

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:1ru1, PDBe:1ru1, PDBj:1ru1
• PDBsum: 1ru1
• PubMed: 14769023
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)