Structure of PDB 6zmj Chain B Binding Site BS01

Receptor Information
>6zmj Chain B (length=649) 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
RHGSPLLIGVRSEHKLSTDHIPILYRTTCLFPVEEKAVEYYFASDASAVI
EHTNRVIFLEDDDVAAVVDGRLSIHRTLQMELQQIMKGNFSSFMQKEIFE
QPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAG
VATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLM
GLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQ
FVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLA
TELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLA
LVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNT
KRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTV
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 chain6zmj 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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PDB6zmj Protein kinase A controls the hexosamine pathway by tuning the feedback inhibition of GFAT-1.
Resolution2.774 Å
Binding residue
(original residue number in PDB)		G375 T376 S377 S421 Q422 S423 T426 S474 E561
Binding residue
(residue number reindexed from 1)		G344 T345 S346 S390 Q391 S392 T395 S443 E530
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 E523 K527 E530 H546 K645
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:6zmj, PDBe:6zmj, PDBj:6zmj
PDBsum6zmj
PubMed33846315
UniProtQ06210|GFPT1_HUMAN Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (Gene Name=GFPT1)

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