Structure of PDB 4m5n Chain B

Receptor sequence

>4m5nB (length=160) Species: 83333 (Escherichia coli K-12)

HMTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQ
DQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDI
MLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILH
TRAFDKLNKW

3D structure

• PDB: 4m5n The identification, analysis and structure-based development of novel inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase.
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R82 R92 D95 D97
• Catalytic site (residue number reindexed from 1): R84 R94 D97 D99
• 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	D95 D97	D97 D99
BS02	MG	B	D95 D97	D97 D99
BS03	APC	B	Q74 R82 R88 R92 D95 D97 I98 R110 L111 T112 H115 Y116 R121	Q76 R84 R90 R94 D97 D99 I100 R112 L113 T114 H117 Y118 R123
BS04	YH7	B	T42 P44 L45 Y53 N55 D95 F123	T44 P46 L47 Y55 N57 D97 F125	MOAD: Kd=7.5uM

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:4m5n, PDBe:4m5n, PDBj:4m5n
• PDBsum: 4m5n
• PubMed: 24613625
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)