Structure of PDB 1ru2 Chain A

Receptor sequence

>1ru2A (length=146) Species: 562 (Escherichia coli)

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPPDYLNA
AVALETSLAPEELLNHTQRIELQQGRGGPRTLDLDIMLFGNEVINTERLT
VPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW

3D structure

• PDB: 1ru2 Essential Roles of a Dynamic Loop in the Catalysis of 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase.
• Chain: A
• Resolution: 1.48 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R92 D95 D97
• Catalytic site (residue number reindexed from 1): R80 D83 D85
• 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	D83 D85
BS02	MG	A	D95 D97	D83 D85
BS03	APC	A	L70 Q74 D95 D97 I98 R110 L111 T112 H115 Y116 R121	L64 Q68 D83 D85 I86 R98 L99 T100 H103 Y104 R109	MOAD: Kd=0.32uM PDBbind-CN: -logKd/Ki=6.49,Kd=0.32uM
BS04	HHR	A	T42 P43 Y53 N55 D95 F123	T42 P43 Y47 N49 D83 F111	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:1ru2, PDBe:1ru2, PDBj:1ru2
• PDBsum: 1ru2
• PubMed: 14769023
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)