Structure of PDB 4m5h Chain A

Receptor sequence

>4m5hA (length=159) Species: 83333 (Escherichia coli K-12)

MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQD
QPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIM
LFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHT
RAFDKLNKW

3D structure

• PDB: 4m5h The identification, analysis and structure-based development of novel inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase.
• Chain: A
• Resolution: 1.11 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R82 R92 D95 D97
• Catalytic site (residue number reindexed from 1): R83 R93 D96 D98
• 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 W89 R92 D95 D97 I98 R110 L111 T112 H115 Y116 R121	L71 Q75 R83 R85 W90 R93 D96 D98 I99 R111 L112 T113 H116 Y117 R122
BS02	YH2	A	T42 P43 L45 G46 Y53 N55 W89 R121 F123	T43 P44 L46 G47 Y54 N56 W90 R122 F124	MOAD: Kd=29uM PDBbind-CN: -logKd/Ki=4.54,Kd=29uM
BS03	CA	A	D95 D97	D96 D98
BS04	CA	A	D95 D97	D96 D98
BS05	CA	A	D49 E87	D50 E88
BS06	CA	A	G26 I28 S31	G27 I29 S32

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:4m5h, PDBe:4m5h, PDBj:4m5h
• PDBsum: 4m5h
• PubMed: 24613625
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)