Structure of PDB 1moq Chain A

Receptor sequence
>1moqA (length=366) Species: 562 (Escherichia coli) [Search protein sequence]
GDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKV
EHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSL
MITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTN
AGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPS
RIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYI
HAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQ
LYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKG
TDVDQPRNLAKSVTVE
3D structure
PDB1moq Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain.
ChainA
Resolution1.57 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E481 K485 E488 H504 K603
Catalytic site (residue number reindexed from 1) E239 K243 E246 H262 K361
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 GLP A T302 S303 S347 Q348 S349 T352 V399 A602 K603 T60 S61 S105 Q106 S107 T110 V157 A360 K361 MOAD: Ki=0.35mM
PDBbind-CN: -logKd/Ki=3.46,Ki=0.35mM
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
View graph for
Biological Process
External links
PDB RCSB:1moq, PDBe:1moq, PDBj:1moq
PDBsum1moq
PubMed9739095
UniProtP17169|GLMS_ECOLI Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (Gene Name=glmS)

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