Structure of PDB 4amv Chain B

Receptor sequence
>4amvB (length=608) Species: 562 (Escherichia coli) [Search protein sequence]
CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGK
VQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGI
IENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIP
QLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVT
RRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRH
YMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILAC
GTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSG
ETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVA
STKAFTTQLTVLLMLVAKLSKLKGLDASIEHDIVHGLQALPSRIEQMLSQ
DKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAG
ELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQD
AGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRN
LAKSVTVE
3D structure
PDB4amv Glutamine Binding Opens the Ammonia Channel and Activates Glucosamine-6P Synthase
ChainB
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C1 R26 G27 W74 N98 G99 Y248 E481 K485 E488 H504 K603
Catalytic site (residue number reindexed from 1) C1 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 F6R B G301 T302 S303 S347 Q348 S349 T352 A400 S401 K485 E488 G301 T302 S303 S347 Q348 S349 T352 A400 S401 K485 E488
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:4amv, PDBe:4amv, PDBj:4amv
PDBsum4amv
PubMed16339762
UniProtP17169|GLMS_ECOLI Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (Gene Name=glmS)

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