Structure of PDB 3ip0 Chain A

Receptor sequence

>3ip0A (length=158) Species: 83333 (Escherichia coli K-12)

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIML
FGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTR
AFDKLNKW

3D structure

• PDB: 3ip0 Dynamic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydroptein pyrophosphokinase: Crystallographic studies
• Chain: A
• Resolution: 0.89 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	MG	A	D95 D97	D95 D97
BS02	MG	A	D95 D97	D95 D97
BS03	APC	A	L70 Q74 R82 R84 W89 R92 D95 D97 I98 R110 L111 T112 H115 Y116 R121	L70 Q74 R82 R84 W89 R92 D95 D97 I98 R110 L111 T112 H115 Y116 R121
BS04	HHR	A	T42 P43 L45 Y53 N55 W89 R92 F123	T42 P43 L45 Y53 N55 W89 R92 F123
BS05	HHS	A	T42 P43 L45 Y53 N55 W89 R92 D95 F123	T42 P43 L45 Y53 N55 W89 R92 D95 F123

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:3ip0, PDBe:3ip0, PDBj:3ip0
• PDBsum: 3ip0
• PubMed: 12578370
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)