Structure of PDB 1eqm Chain A

Receptor sequence
>1eqmA (length=158) Species: 562 (Escherichia coli) [Search protein sequence]
TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIML
FGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTR
AFDKLNKW
3D structure
PDB1eqm Unusual conformational changes in 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as revealed by X-ray crystallography and NMR.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 E77 L96 E77 L96
BS02 ADP A L70 D97 I98 R110 L111 T112 L70 D97 I98 R110 L111 T112
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1eqm, PDBe:1eqm, PDBj:1eqm
PDBsum1eqm
PubMed11546767
UniProtP26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)

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