Structure of PDB 4ndn Chain B Binding Site BS02

Receptor Information
>4ndn Chain B (length=383) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKT
GMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQ
QSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNA
KLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEE
VCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLT
GRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCR
RVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVR
DLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
Ligand information
Ligand IDSAM
InChIInChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/t7-,8+,10+,11+,14+,27-/m0/s1
InChIKeyMEFKEPWMEQBLKI-FCKMPRQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[S@@+](CC[C@H](N)C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S+](CCC(C(=O)[O-])N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341C[S+](CC[CH](N)C([O-])=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S@@+](CC[C@@H](C(=O)[O-])N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
ACDLabs 10.04[O-]C(=O)C(N)CC[S+](C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H22 N6 O5 S
NameS-ADENOSYLMETHIONINE
ChEMBLCHEMBL1235831
DrugBank
ZINC
PDB chain4ndn Chain A Residue 407 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4ndn Structure and function study of the complex that synthesizes S-adenosylmethionine.
Resolution2.34 Å
Binding residue
(original residue number in PDB)		E70 Q113 D116 I117
Binding residue
(residue number reindexed from 1)		E58 Q101 D104 I105
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H29 D31 K32 E57 E70 K181 F250 D258 A259 R264 K265 K285 K289 D291
Catalytic site (residue number reindexed from 1) H17 D19 K20 E45 E58 K169 F238 D246 A247 R252 K253 K273 K277 D279
Enzyme Commision number 2.5.1.6: methionine adenosyltransferase.
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:4ndn, PDBe:4ndn, PDBj:4ndn
PDBsum4ndn
PubMed25075345
UniProtP31153|METK2_HUMAN S-adenosylmethionine synthase isoform type-2 (Gene Name=MAT2A)

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