Structure of PDB 1tmm Chain A

Receptor sequence

>1tmmA (length=158) Species: 562 (Escherichia coli)

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERAGPRTLDLDIML
FGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTR
AFDKLNKW

3D structure

• PDB: 1tmm Is the Critical Role of Loop 3 of Escherichia coli 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase in Catalysis Due to Loop-3 Residues Arginine-84 and Tryptophan-89? Site-Directed Mutagenesis, Biochemical, and Crystallographic Studies.
• Chain: A
• Resolution: 1.25 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	MG	A	G26 S31	G26 S31
BS04	APC	A	Q74 R82 K85 A86 D95 D97 I98 R110 L111 T112 H115 Y116 R121	Q74 R82 K85 A86 D95 D97 I98 R110 L111 T112 H115 Y116 R121	MOAD: Kd=0.23uM PDBbind-CN: -logKd/Ki=6.64,Kd=0.23uM
BS05	HHR	A	T42 P43 L45 Y53 N55 D95 F123	T42 P43 L45 Y53 N55 D95 F123	MOAD: Kd=1.1uM

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:1tmm, PDBe:1tmm, PDBj:1tmm
• PDBsum: 1tmm
• PubMed: 15952765
• UniProt: P26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)