Structure of PDB 6svq Chain A Binding Site BS02

Receptor Information
>6svq Chain A (length=651) 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
QSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCEVHINAGPEIG
VASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVL
SMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGIL
AGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICD
KEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFP
R
Ligand information
Ligand IDGLU
InChIInChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10)/t3-/m0/s1
InChIKeyWHUUTDBJXJRKMK-VKHMYHEASA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)C(N)CCC(=O)O
OpenEye OEToolkits 1.7.0C(CC(=O)O)C(C(=O)O)N
OpenEye OEToolkits 1.7.0C(CC(=O)O)[C@@H](C(=O)O)N
CACTVS 3.370N[C@@H](CCC(O)=O)C(O)=O
CACTVS 3.370N[CH](CCC(O)=O)C(O)=O
FormulaC5 H9 N O4
NameGLUTAMIC ACID
ChEMBLCHEMBL575060
DrugBankDB00142
ZINCZINC000001482113
PDB chain6svq Chain A Residue 702 [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)		R95 W96 T98 N123 G124 D148
Binding residue
(residue number reindexed from 1)		R94 W95 T97 N122 G123 D147
Annotation score5
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

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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