Structure of PDB 7dnr Chain A

Receptor sequence
>7dnrA (length=357) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
GDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKV
EHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSL
MITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTN
AGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPS
RIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYI
HAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQ
LYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKG
TDVDQPR
3D structure
PDB7dnr Discovery of Metal-binding Proteins by Thermal Proteome Profiling
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.16: glutamine--fructose-6-phosphate transaminase (isomerizing).
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 ZN A H466 H467 H223 H224
Gene Ontology
Molecular Function
GO:0004360 glutamine-fructose-6-phosphate transaminase (isomerizing) activity
GO:0097367 carbohydrate derivative binding
Biological Process
GO:1901135 carbohydrate derivative metabolic process
GO:1901137 carbohydrate derivative biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:7dnr, PDBe:7dnr, PDBj:7dnr
PDBsum7dnr
PubMed
UniProtP17169|GLMS_ECOLI Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (Gene Name=glmS)

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