Structure of PDB 3o61 Chain A

Receptor sequence
>3o61A (length=187) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MTQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATI
LLYNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKA
AIEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRANAGGEDIE
VLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD
3D structure
PDB3o61 Structural studies of the Nudix GDP-mannose hydrolase from E. coli reveals a new motif for mannose recognition.
ChainA
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 A Y17 G47 R67 A85 G86 L87 E127 K176 Y17 G47 R67 A85 G86 L87 E127 K172
BS02 MG A A85 E104 A85 E104
BS03 GDD A K38 R39 E40 P122 K38 R39 E40 P122
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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