Structure of PDB 1mos Chain A Binding Site BS01

Receptor Information
>1mos Chain A (length=367) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSK
VEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNS
LMITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMT
NAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALP
SRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISY
IHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGG
QLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIK
GTDVDQPRNLAKSVTVE
Ligand information
Ligand IDAGP
InChIInChI=1S/C6H16NO8P/c7-3(1-8)5(10)6(11)4(9)2-15-16(12,13)14/h3-6,8-11H,1-2,7H2,(H2,12,13,14)/t3-,4+,5+,6+/m0/s1
InChIKeyLBNVXZROMBUNNQ-SLPGGIOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C([C@@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)N)O
CACTVS 3.341N[C@@H](CO)[C@@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O
OpenEye OEToolkits 1.5.0C(C(C(C(C(COP(=O)(O)O)O)O)O)N)O
CACTVS 3.341N[CH](CO)[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)C(O)C(N)CO
FormulaC6 H16 N O8 P
Name2-DEOXY-2-AMINO GLUCITOL-6-PHOSPHATE
ChEMBLCHEMBL396380
DrugBankDB02445
ZINCZINC000003870803
PDB chain1mos Chain A Residue 609 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1mos The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		T302 S303 S347 Q348 S349 T352 K485 E488
Binding residue
(residue number reindexed from 1)		T61 S62 S106 Q107 S108 T111 K244 E247
Annotation score1
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).
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:1mos, PDBe:1mos, PDBj:1mos
PDBsum1mos
PubMed10091662
UniProtP17169|GLMS_ECOLI Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (Gene Name=glmS)

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