Structure of PDB 3o61 Chain C

Receptor sequence
>3o61C (length=182) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATIL
LYNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKAA
IEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRAEDIEVLELP
FSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD
3D structure
PDB3o61 Structural studies of the Nudix GDP-mannose hydrolase from E. coli reveals a new motif for mannose recognition.
ChainC
Resolution2.45 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.1.-
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 GDD C Y17 F18 R67 A85 G86 L87 E127 K176 Y16 F17 R66 A84 G85 L86 E126 K167
BS02 MG C A85 E104 A84 E103
BS03 GDD C K38 R39 E40 P122 K37 R38 E39 P121
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0052751 GDP-mannose hydrolase activity
Biological Process
GO:0006753 nucleoside phosphate metabolic process
GO:0019693 ribose phosphate metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3o61, PDBe:3o61, PDBj:3o61
PDBsum3o61
PubMed21638333
UniProtP37128|NUDK_ECOLI GDP-mannose pyrophosphatase (Gene Name=nudK)

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