Structure of PDB 2o5w Chain A

Receptor sequence
>2o5wA (length=147) Species: 562 (Escherichia coli) [Search protein sequence]
KDKVYKRPVSILVVIYAQDTKRVLMLQRRDDPDFWQSVTGSVEEGETAPQ
AAMREVKEEVTIDVVAEQLTLIDCQRTVEFEIFSHLRHRYAPGVTRNTES
WFCLALPHERQIVFTEHLAYKWLDAPAAAALTKSWSNRQAIEQFVIN
3D structure
PDB2o5w Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis.
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.1.67: dihydroneopterin triphosphate diphosphatase.
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 PPV A K7 R29 T40 K6 R28 T39
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008828 dATP diphosphatase activity
GO:0016787 hydrolase activity
GO:0019177 dihydroneopterin triphosphate pyrophosphohydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2o5w, PDBe:2o5w, PDBj:2o5w
PDBsum2o5w
PubMed17698004
UniProtP0AFC0|NUDB_ECOLI Dihydroneopterin triphosphate diphosphatase (Gene Name=nudB)

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