Structure of PDB 5hil Chain A

Receptor sequence
>5hilA (length=240) Species: 523843 (Methanohalophilus portucalensis FDF-1) [Search protein sequence]
DHYEEEYVLGFVDKWDELIDWESRAESEGDTIINILKERGVKKVLDVATG
TGFNSVRLLQAGFDVVSADGSAEMLVKAFDNARDHGYLMRTVQADWRWMN
KDIHDKFDAIVCLGNSFTHLFDEGDRRKALAEFYALLKHDGVLLLDQRNY
DAILDSKHAHYYCGDTVSVYPEHVDEGLARFKYEFSDGSVYNLNMFPLRK
DYTRQLLHEVGFQEINTLGDFKETYKEDEPDFFLHVAEKN
3D structure
PDB5hil Structural Analysis of Glycine Sarcosine N-methyltransferase from Methanohalophilus portucalensis Reveals Mechanistic Insights into the Regulation of Methyltransferase Activity
ChainA
Resolution2.471 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y26 G133 H138 R167 Y185
Catalytic site (residue number reindexed from 1) Y7 G114 H119 R148 Y162
Enzyme Commision number 2.1.1.156: glycine/sarcosine N-methyltransferase.
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 SAH A R43 A67 G69 N73 D88 G89 D114 W115 L132 S135 R24 A48 G50 N54 D69 G70 D95 W96 L113 S116
BS02 SAR A N134 H138 R167 Y206 N115 H119 R148 Y183
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0016594 glycine binding
GO:0016740 transferase activity
GO:0017174 glycine N-methyltransferase activity
GO:0042802 identical protein binding
GO:1904047 S-adenosyl-L-methionine binding
Biological Process
GO:0006111 regulation of gluconeogenesis
GO:0006730 one-carbon metabolic process
GO:0032259 methylation
GO:0046498 S-adenosylhomocysteine metabolic process
GO:0046500 S-adenosylmethionine metabolic process
GO:0051289 protein homotetramerization
GO:1901052 sarcosine metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:5hil, PDBe:5hil, PDBj:5hil
PDBsum5hil
PubMed27934872
UniProtF6KV61

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