Structure of PDB 6svq Chain B Binding Site BS01

Receptor Information
>6svq Chain B (length=640) 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
RRGSPLLIGVRSEHKLSTDHIPILYRTTCLFPVEEKAVEYYFASDASAVI
EHTNRVIFLEDDDVAAVVDGRLSIHRELQQIMKGNFSSFMQKEIFEQPES
VVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATR
QVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRY
CKERGALTVGITNTVGSSISRETDCEVHINAGPEIGVASTKAYTSQFVSL
VMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELY
HQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDK
LMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTI
KVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLA
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 chain6svq Chain B Residue 701 [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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PDB6svq Loss of GFAT-1 feedback regulation activates the hexosamine pathway that modulates protein homeostasis.
Resolution2.717 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)		G340 T341 S342 S386 Q387 S388 T391 S439 K523 E526
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) L8 R33 W96 N123 G124 E554 K558 E561 H577
Catalytic site (residue number reindexed from 1) L7 R32 W95 N122 G123 E519 K523 E526 H542
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:6svq, PDBe:6svq, PDBj:6svq
PDBsum6svq
PubMed32019926
UniProtQ06210|GFPT1_HUMAN Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (Gene Name=GFPT1)

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