Structure of PDB 6s83 Chain B

Receptor sequence
>6s83B (length=400) Species: 186497 (Pyrococcus furiosus DSM 3638) [Search protein sequence]
ARNIVVEEIVRTPVEMQQVELVERKGIGHPDSIADGIAEAVSRALCREYI
RRYGVILHHNTDQVEVVGGRAYPRFGGGEVVKPIYILLSGRAVELVDQEL
FPVHEVAIKAAKNYLKNAIRHLDVENHVIIDSRIGQGSVDLVSVFNKARE
NPIPLANDTSFGVGYAPLSETERLVLETEKLLNSEKFKKEYPAVGEDIKV
MGLRRGNEIDLTIAAAIVDSEVATPKEYLEVKDKIKEAVEELAKEITSRK
VNIYVNTADDPERGIYYITVTGTSAEAGDDGSVGRGNRVNGLITPNRHMS
MEAAAGKNPVSHVGKIYNILAMLIAEDIAKTLPVEEVYVRILSQIGKPID
QPLVASIQVIPKPGHSVKEFEKDAYSIADEWLANITKVQKMILEDKISVF
3D structure
PDB6s83 Structures of catalytic cycle intermediates of the Pyrococcus furiosus methionine adenosyltransferase demonstrate negative cooperativity in the archaeal orthologues.
ChainB
Resolution2.336 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 MDN B D159 E303 K308 H313 D158 E302 K307 H312
BS02 SAM B H59 N61 D141 L142 D159 H58 N60 D140 L141 D158
BS03 MG B D63 Q64 D62 Q63
BS04 ACP B K26 H30 D198 K200 A215 Y268 S275 K25 H29 D197 K199 A214 Y267 S274
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
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Biological Process
External links
PDB RCSB:6s83, PDBe:6s83, PDBj:6s83
PDBsum6s83
PubMed31962159
UniProtQ8TZW1|METK_PYRFU S-adenosylmethionine synthase (Gene Name=mat)

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