Structure of PDB 6svp Chain A Binding Site BS02

Receptor Information
>6svp Chain A (length=653) 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
IEHTNRVIFLEDDDVAAVVDGRLSIHRIKHPGRAVQTLQMELQQIMKGNF
SSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLIL
IACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLS
QSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIG
VASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVL
SMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGIL
AGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICD
KEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFP
RNL
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 chain6svp Chain A Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		S455 R456 T458
Binding residue
(residue number reindexed from 1)		S434 R435 T437
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 E533 K537 E540 H556
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
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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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