Structure of PDB 3ooj Chain B

Receptor sequence
>3oojB (length=608) Species: 562 (Escherichia coli) [Search protein sequence]
AGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGK
VQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGI
IENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIP
QLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVT
RRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRH
YMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILAC
GTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSG
ETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVA
STKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQ
DKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAG
ELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQD
AGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRN
LAKSVTVE
3D structure
PDB3ooj Structural basis for morpheein-type allosteric regulation of Escherichia coli glucosamine-6-phosphate synthase: equilibrium between inactive hexamer and active dimer.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 Y248 E481 K485 E488 H504 K603
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 B R333 K334 R333 K334
BS02 GLU B A1 R73 W74 T76 N98 G99 D123 A1 R73 W74 T76 N98 G99 D123
BS03 G6P B C300 T302 S347 Q348 S349 T352 V399 A602 C300 T302 S347 Q348 S349 T352 V399 A602
BS04 G6Q B D474 Q475 E569 D474 Q475 E569
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
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)

[Back to BioLiP]