Structure of PDB 3kuh Chain A

Receptor sequence

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

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIML
FGNEVINTERLTVPAYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTR
AFDKLNKW

3D structure

• PDB: 3kuh Catalytic center assembly of HPPK as revealed by the crystal structure of a ternary complex at 1.25 A resolution
• Chain: A
• Resolution: 1.35 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	APC	A	L70 Q74 R82 R84 R92 D95 D97 I98 R110 L111 T112 Y116 R121	L70 Q74 R82 R84 R92 D95 D97 I98 R110 L111 T112 Y116 R121
BS02	PH2	A	T42 P43 L45 Y53 N55 W89 R92 F123	T42 P43 L45 Y53 N55 W89 R92 F123
BS03	MG	A	D95 D97	D95 D97
BS04	MG	A	D95 D97	D95 D97

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