Structure of PDB 5fwa Chain A

Receptor sequence
>5fwaA (length=339) Species: 10090 (Mus musculus) [Search protein sequence]
DTWQDEEYFDSYGTLKLHLEMLADQPRTTKYHSVILQNKESLKDKVILDV
GCGTGIISLFCAHHARPKAVYAVEASDMAQHTSQLVLQNGFADTITVFQQ
KVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDTWLKGDGIIWPTT
AALHLVPCSAEKDYHSKVLFWDNAYEFNLSALKSLAIKEFFSRPKSNHIL
KPEDCLSEPCTILQLDMRTVQVPDLETMRGELRFDIQKAGTLHGFTAWFS
VYFQSLEEGQPQQVLSTGPLHPTTHWKQTLFMMDDPVPVHTGDVVTGSVV
LQRNPVWRRHMSVSLSWVVTSALDPTSQRVGEKVFPIWW
3D structure
PDB5fwa Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D130 E223 E232 H381
Catalytic site (residue number reindexed from 1) D24 E117 E126 H275
Enzyme Commision number 2.1.1.125: Transferred entry: 2.1.1.319, 2.1.1.320, 2.1.1.321 and 2.1.1.322.
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 J7C A Y114 F115 Y118 G157 E180 A181 K207 E223 W224 M225 E232 M234 S237 Y8 F9 Y12 G51 E74 A75 K101 E117 W118 M119 E126 M128 S131 MOAD: ic50=16.3uM
PDBbind-CN: -logKd/Ki=4.79,IC50=16.3uM
BS02 CA A G196 D199 G90 D93
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0016274 protein-arginine N-methyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0018216 peptidyl-arginine methylation
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5fwa, PDBe:5fwa, PDBj:5fwa
PDBsum5fwa
PubMed27879050
UniProtQ3UKX1

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