Structure of PDB 6svp Chain B Binding Site BS03

Receptor Information
>6svp Chain B (length=652) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWE
ANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGE
PSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTET
IAKLVKYMYDNRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGT
RRGSPLLIGVRSEHKLSTDHIPILYTTCLFPVEEKAVEYYFASDASAVIE
HTNRVIFLEDDDVAAVVDGRLSIHRAVQTLQMELQQIMKGNFSSFMQKEI
FEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYH
AGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADT
LMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYT
SQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQK
LATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGP
LALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIK
NTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVT
VE
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 chain6svp Chain B Residue 703 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6svp Loss of GFAT-1 feedback regulation activates the hexosamine pathway that modulates protein homeostasis.
Resolution2.531 Å
Binding residue
(original residue number in PDB)		G375 T376 S377 S421 Q422 S423 T426 S474 K558 E561
Binding residue
(residue number reindexed from 1)		G346 T347 S348 S392 Q393 S394 T397 S445 K529 E532
Annotation score1
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).
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)

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