Structure of PDB 8qdz Chain A

Receptor sequence
>8qdzA (length=380) Species: 9606 (Homo sapiens) [Search protein sequence]
GTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMI
LLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSP
DIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLA
ELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCL
DEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRK
IIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVL
VQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLD
LKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
3D structure
PDB8qdz Development of a Series of Pyrrolopyridone MAT2A Inhibitors.
ChainA
Resolution1.16 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.6: methionine adenosyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 U6R A F18 F20 Q190 W274 F3 F5 Q175 W259
BS02 SAM A H29 P30 D179 K181 S247 F250 D258 H14 P15 D164 K166 S232 F235 D243
Gene Ontology
Molecular Function
GO:0004478 methionine adenosyltransferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0036094 small molecule binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006556 S-adenosylmethionine biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0034214 protein hexamerization
GO:0051291 protein heterooligomerization
GO:0061431 cellular response to methionine
GO:1904263 positive regulation of TORC1 signaling
GO:1990830 cellular response to leukemia inhibitory factor
Cellular Component
GO:0005829 cytosol
GO:0048269 methionine adenosyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8qdz, PDBe:8qdz, PDBj:8qdz
PDBsum8qdz
PubMed38466661
UniProtP31153|METK2_HUMAN S-adenosylmethionine synthase isoform type-2 (Gene Name=MAT2A)

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