Structure of PDB 6svp Chain B

Receptor sequence
>6svpB (length=652) Species: 9606 (Homo sapiens) [Search protein sequence]
CGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWE
ANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGE
PSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTET
IAKLVKYMYDNRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGT
RRGSPLLIGVRSEHKLSTDHIPILYTTCLFPVEEKAVEYYFASDASAVIE
HTNRVIFLEDDDVAAVVDGRLSIHRAVQTLQMELQQIMKGNFSSFMQKEI
FEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYH
AGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADT
LMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYT
SQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQK
LATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGP
LALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIK
NTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVT
VE
3D structure
PDB6svp Loss of GFAT-1 feedback regulation activates the hexosamine pathway that modulates protein homeostasis.
ChainB
Resolution2.531 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) L8 R33 W96 N123 G124 E554 K558 E561 H577 K676
Catalytic site (residue number reindexed from 1) L7 R32 W95 N122 G123 E525 K529 E532 H548 K647
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 UD1 B R343 G354 G355 G445 T447 S455 T458 C460 G461 V462 H463 R314 G325 G326 G416 T418 S426 T429 C431 G432 V433 H434
BS02 MG B S455 R456 T458 S426 R427 T429
BS03 G6Q B G375 T376 S377 S421 Q422 S423 T426 S474 K558 E561 G346 T347 S348 S392 Q393 S394 T397 S445 K529 E532
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:6svp, PDBe:6svp, PDBj:6svp
PDBsum6svp
PubMed32019926
UniProtQ06210|GFPT1_HUMAN Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (Gene Name=GFPT1)

[Back to BioLiP]