Structure of PDB 6s83 Chain B Binding Site BS03
Receptor Information
>6s83 Chain B (length=400) Species:
186497
(Pyrococcus furiosus DSM 3638) [
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ARNIVVEEIVRTPVEMQQVELVERKGIGHPDSIADGIAEAVSRALCREYI
RRYGVILHHNTDQVEVVGGRAYPRFGGGEVVKPIYILLSGRAVELVDQEL
FPVHEVAIKAAKNYLKNAIRHLDVENHVIIDSRIGQGSVDLVSVFNKARE
NPIPLANDTSFGVGYAPLSETERLVLETEKLLNSEKFKKEYPAVGEDIKV
MGLRRGNEIDLTIAAAIVDSEVATPKEYLEVKDKIKEAVEELAKEITSRK
VNIYVNTADDPERGIYYITVTGTSAEAGDDGSVGRGNRVNGLITPNRHMS
MEAAAGKNPVSHVGKIYNILAMLIAEDIAKTLPVEEVYVRILSQIGKPID
QPLVASIQVIPKPGHSVKEFEKDAYSIADEWLANITKVQKMILEDKISVF
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
6s83 Chain B Residue 503 [
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Receptor-Ligand Complex Structure
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PDB
6s83
Structures of catalytic cycle intermediates of the Pyrococcus furiosus methionine adenosyltransferase demonstrate negative cooperativity in the archaeal orthologues.
Resolution
2.336 Å
Binding residue
(original residue number in PDB)
D63 Q64
Binding residue
(residue number reindexed from 1)
D62 Q63
Annotation score
1
Enzymatic activity
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:0016740
transferase activity
Biological Process
GO:0006556
S-adenosylmethionine biosynthetic process
GO:0006730
one-carbon metabolic process
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Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:6s83
,
PDBe:6s83
,
PDBj:6s83
PDBsum
6s83
PubMed
31962159
UniProt
Q8TZW1
|METK_PYRFU S-adenosylmethionine synthase (Gene Name=mat)
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