Structure of PDB 6svm Chain B Binding Site BS03

Receptor Information
>6svm Chain B (length=655) 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
RRGSPLLIGVRSEHKLSTDHIPILYRSTTCLFPVEEKAVEYYFASDASAV
IEHTNRVIFLEDDDVAAVVDGRLSIHRRAVQTLQMELQQIMKGNFSSFMQ
KEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGT
SYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGET
ADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTK
AYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDE
IQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELK
HGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTE
TIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAK
SVTVE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain6svm 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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PDB6svm Loss of GFAT-1 feedback regulation activates the hexosamine pathway that modulates protein homeostasis.
Resolution2.481 Å
Binding residue
(original residue number in PDB)		S455 R456 T458
Binding residue
(residue number reindexed from 1)		S429 R430 T432
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 E528 K532 E535 H551 K650
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6svm, PDBe:6svm, PDBj:6svm
PDBsum6svm
PubMed32019926
UniProtQ06210|GFPT1_HUMAN Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (Gene Name=GFPT1)

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