Structure of PDB 3ooj Chain F

Receptor sequence
>3oojF (length=594) Species: 562 (Escherichia coli) [Search protein sequence]
AGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGK
VQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGI
IENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIP
QLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVT
RRFIFLEEGDIAEITRRSVNIFDKTGAEVKKGIYRHYMQKEIYEQPNAIK
NTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWF
ESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKE
LGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLM
LVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDK
HHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADM
PVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSDNMHIIEM
PHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE
3D structure
PDB3ooj Structural basis for morpheein-type allosteric regulation of Escherichia coli glucosamine-6-phosphate synthase: equilibrium between inactive hexamer and active dimer.
ChainF
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
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 G6Q F R333 K334 R319 K320
BS02 GLU F A1 R73 W74 T76 H77 H86 G99 D123 A1 R73 W74 T76 H77 H86 G99 D123
BS03 G6P F C300 T302 S303 S347 Q348 S349 T352 V399 A602 K603 C286 T288 S289 S333 Q334 S335 T338 V385 A588 K589
BS04 G6Q F D474 Q475 E569 A572 D460 Q461 E555 A558
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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