Structure of PDB 3o61 Chain D

Receptor sequence
>3o61D (length=190) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATIL
LYNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKAA
IEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRANAGGGVEDE
DIEVLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD
3D structure
PDB3o61 Structural studies of the Nudix GDP-mannose hydrolase from E. coli reveals a new motif for mannose recognition.
ChainD
Resolution2.45 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D K38 R39 E40 P122 K37 R38 E39 P121
BS02 GDD D Y17 R67 A85 G86 L87 E127 D150 E151 K176 Y16 R66 A84 G85 L86 E126 D149 E150 K175
BS03 MG D A85 E104 A84 E103
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

View graph for
Molecular Function

View graph for
Biological Process

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

[Back to BioLiP]