Structure of PDB 4m5j Chain A

Receptor sequence

>4m5jA (length=157) Species: 83333 (Escherichia coli K-12)

MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQD
QPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRERWGPRTLDLDIMLF
GNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRA
FDKLNKW

3D structure

• PDB: 4m5j The identification, analysis and structure-based development of novel inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase.
• Chain: A
• Resolution: 1.696 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R82 R92 D95 D97
• Catalytic site (residue number reindexed from 1): R83 R91 D94 D96
• 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	Q74 R82 W89 R92 D95 D97 I98 R110 L111 T112 H115 R121	Q75 R83 W88 R91 D94 D96 I97 R109 L110 T111 H114 R120
BS02	YH5	A	T42 P43 P44 L45 Y53 N55 W89 R92 R121 F123	T43 P44 P45 L46 Y54 N56 W88 R91 R120 F122	MOAD: Kd=14.5uM PDBbind-CN: -logKd/Ki=4.84,Kd=14.5uM BindingDB: IC50=44000nM,Kd=14500nM
BS03	MG	A	D95 D97	D94 D96
BS04	MG	A	D95 D97	D94 D96

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:4m5j, PDBe:4m5j, PDBj:4m5j
• PDBsum: 4m5j
• PubMed: 24613625
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)