Structure of PDB 6svo Chain A Binding Site BS01

Receptor Information
>6svo Chain A (length=663) 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
RRGSPLLIGVRSEHKLSTDHIPILYRRVDSTTCLFPVEEKAVEYYFASDA
SAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIDHPGRAVQTLQMELQQIMK
GNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRR
LILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCF
FLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGP
EIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIK
EVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSE
GILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVV
ICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDV
DFPRNLAKSVTVE
Ligand information
Ligand IDAGP
InChIInChI=1S/C6H16NO8P/c7-3(1-8)5(10)6(11)4(9)2-15-16(12,13)14/h3-6,8-11H,1-2,7H2,(H2,12,13,14)/t3-,4+,5+,6+/m0/s1
InChIKeyLBNVXZROMBUNNQ-SLPGGIOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C([C@@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)N)O
CACTVS 3.341N[C@@H](CO)[C@@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O
OpenEye OEToolkits 1.5.0C(C(C(C(C(COP(=O)(O)O)O)O)O)N)O
CACTVS 3.341N[CH](CO)[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)C(O)C(N)CO
FormulaC6 H16 N O8 P
Name2-DEOXY-2-AMINO GLUCITOL-6-PHOSPHATE
ChEMBLCHEMBL396380
DrugBankDB02445
ZINCZINC000003870803
PDB chain6svo Chain A 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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PDB6svo Loss of GFAT-1 feedback regulation activates the hexosamine pathway that modulates protein homeostasis.
Resolution2.328 Å
Binding residue
(original residue number in PDB)		C374 T376 S421 Q422 S423 T426 S474 K558 E561
Binding residue
(residue number reindexed from 1)		C356 T358 S403 Q404 S405 T408 S456 K540 E543
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 E536 K540 E543 H559 K658
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:6svo, PDBe:6svo, PDBj:6svo
PDBsum6svo
PubMed32019926
UniProtQ06210|GFPT1_HUMAN Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (Gene Name=GFPT1)

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