Structure of PDB 7dnr Chain A Binding Site BS01

Receptor Information
>7dnr Chain A (length=357) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKV
EHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSL
MITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTN
AGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPS
RIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYI
HAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQ
LYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKG
TDVDQPR
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain7dnr Chain A Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7dnr Discovery of Metal-binding Proteins by Thermal Proteome Profiling
Resolution1.7 Å
Binding residue
(original residue number in PDB)		H466 H467
Binding residue
(residue number reindexed from 1)		H223 H224
Annotation score1
Enzymatic activity
Enzyme Commision number 2.6.1.16: glutamine--fructose-6-phosphate transaminase (isomerizing).
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

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Molecular Function
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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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