Structure of PDB 1mos Chain A

Receptor sequence
>1mosA (length=367) Species: 562 (Escherichia coli) [Search protein sequence]
AGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSK
VEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNS
LMITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMT
NAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALP
SRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISY
IHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGG
QLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIK
GTDVDQPRNLAKSVTVE
3D structure
PDB1mos The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase.
ChainA
Resolution2.0 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) E240 K244 E247 H263 K362
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 AGP A T302 S303 S347 Q348 S349 T352 K485 E488 T61 S62 S106 Q107 S108 T111 K244 E247
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:1mos, PDBe:1mos, PDBj:1mos
PDBsum1mos
PubMed10091662
UniProtP17169|GLMS_ECOLI Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (Gene Name=glmS)

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