Structure of PDB 1o92 Chain A Binding Site BS04

Receptor Information
>1o92 Chain A (length=368) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GAFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMV
LLCGEITSMAMIDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSP
EDVGAGDQGLMFGYATDETEECMPLTIVLAHKLNTRMADLRRSGVLPWLR
PDSKTQVTVQYVQDNGAVIPVRVHTIVISVQHNEDITLEAMREALKEQVI
KAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAH
GGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVSYAIGVAEP
LSISIFTYGTSKKTERELLEVVNKNFDLRPGVIVRDLDLKKPIYQKTACY
GHFGRSEFPWEVPKKLVF
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1o92 Chain A Residue 1404 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1o92 Crystal Structures of Methionine Adenosyltransferase Complexed with Substrates and Products Reveal the Methionine-ATP Recognition and Give Insights Into the Catalytic Mechanism
Resolution3.19 Å
Binding residue
(original residue number in PDB)		E24 K266
Binding residue
(residue number reindexed from 1)		E8 K238
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H30 D32 K33 E58 E71 K182 F251 D259 A260 R265 K266 K286 K290 D292
Catalytic site (residue number reindexed from 1) H14 D16 K17 E42 E55 K154 F223 D231 A232 R237 K238 K258 K262 D264
Enzyme Commision number 2.5.1.6: methionine adenosyltransferase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004478 methionine adenosyltransferase activity
GO:0005524 ATP binding
GO:0016597 amino acid binding
GO:0016740 transferase activity
GO:0042802 identical protein binding
GO:0043531 ADP binding
GO:0046872 metal ion binding
Biological Process
GO:0006556 S-adenosylmethionine biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0009087 methionine catabolic process
GO:0051289 protein homotetramerization
GO:0065003 protein-containing complex assembly
Cellular Component
GO:0005829 cytosol
GO:0016363 nuclear matrix
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:1o92, PDBe:1o92, PDBj:1o92
PDBsum1o92
PubMed12888348
UniProtP13444|METK1_RAT S-adenosylmethionine synthase isoform type-1 (Gene Name=Mat1a)

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