Structure of PDB 3o61 Chain B

Receptor sequence
>3o61B (length=187) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATILL
YNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKAAI
EETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRANAGGGVEDIE
VLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD
3D structure
PDB3o61 Structural studies of the Nudix GDP-mannose hydrolase from E. coli reveals a new motif for mannose recognition.
ChainB
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 B K38 R39 E40 P122 K36 R37 E38 P120
BS02 GDD B Y17 F18 G47 R67 A85 G86 L87 E127 E151 K176 Y15 F16 G45 R65 A83 G84 L85 E125 E147 K172
BS03 MG B A85 E104 A83 E102
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]