Structure of PDB 1ru1 Chain B

Receptor sequence

>1ru1B (length=152) Species: 562 (Escherichia coli)

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRGGPRTLDLDIMLFGNEVI
NTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLN
KW

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): R292 D295 D297
• Catalytic site (residue number reindexed from 1): R86 D89 D91
• 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	B	D295 D297	D89 D91
BS02	MG	B	D295 D297	D89 D91
BS03	APC	B	L270 D295 D297 I298 R310 L311 T312 H315 Y316 R321	L70 D89 D91 I92 R104 L105 T106 H109 Y110 R115
BS04	PH2	B	T242 P243 L245 Y253 N255 D295 F323	T42 P43 L45 Y53 N55 D89 F117	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)