Structure of PDB 7rxw Chain A

Receptor sequence
>7rxwA (length=381) Species: 9606 (Homo sapiens) [Search protein sequence]
EGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGM
ILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQS
PDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKL
AELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVC
LDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGR
KIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRV
LVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDL
DLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
3D structure
PDB7rxw Mechanism of Triphosphate Hydrolysis by Human MAT2A at 1.07 angstrom Resolution.
ChainA
Resolution1.07 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 MTA A H29 P30 D179 K181 S247 F250 D258 H15 P16 D165 K167 S233 F236 D244
BS02 2PN A H29 K181 K265 H15 K167 K251
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:7rxw, PDBe:7rxw, PDBj:7rxw
PDBsum7rxw
PubMed34668717
UniProtP31153|METK2_HUMAN S-adenosylmethionine synthase isoform type-2 (Gene Name=MAT2A)

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