Structure of PDB 3ooj Chain F Binding Site BS01

Receptor Information
>3ooj Chain F (length=594) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGK
VQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGI
IENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIP
QLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVT
RRFIFLEEGDIAEITRRSVNIFDKTGAEVKKGIYRHYMQKEIYEQPNAIK
NTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWF
ESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKE
LGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLM
LVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDK
HHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADM
PVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSDNMHIIEM
PHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE
Ligand information
Ligand IDG6Q
InChIInChI=1S/C6H13O9P/c7-1-3(8)5(10)6(11)4(9)2-15-16(12,13)14/h1,3-6,8-11H,2H2,(H2,12,13,14)/t3-,4+,5+,6+/m0/s1
InChIKeyVFRROHXSMXFLSN-SLPGGIOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)C(O)C(O)C=O
OpenEye OEToolkits 1.5.0C(C(C(C(C(C=O)O)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0C([C@H]([C@H]([C@@H]([C@H](C=O)O)O)O)O)OP(=O)(O)O
CACTVS 3.341O[CH](CO[P](O)(O)=O)[CH](O)[CH](O)[CH](O)C=O
CACTVS 3.341O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H](O)[C@@H](O)C=O
FormulaC6 H13 O9 P
NameGLUCOSE-6-PHOSPHATE
ChEMBL
DrugBankDB03581
ZINCZINC000019850142
PDB chain3ooj Chain E Residue 610 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3ooj Structural basis for morpheein-type allosteric regulation of Escherichia coli glucosamine-6-phosphate synthase: equilibrium between inactive hexamer and active dimer.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		R333 K334
Binding residue
(residue number reindexed from 1)		R319 K320
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) A1 R26 G27 W74 N98 G99 Y248 E481 K485 E488 H504 K603
Catalytic site (residue number reindexed from 1) A1 R26 G27 W74 N98 G99 Y234 E467 K471 E474 H490 K589
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:0005515 protein binding
GO:0008483 transaminase activity
GO:0097367 carbohydrate derivative binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006047 UDP-N-acetylglucosamine metabolic process
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0006487 protein N-linked glycosylation
GO:0006541 glutamine metabolic process
GO:1901135 carbohydrate derivative metabolic process
GO:1901137 carbohydrate derivative biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ooj, PDBe:3ooj, PDBj:3ooj
PDBsum3ooj
PubMed22851174
UniProtP17169|GLMS_ECOLI Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (Gene Name=glmS)

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