Structure of PDB 5ful Chain A

Receptor sequence
>5fulA (length=339) Species: 10090 (Mus musculus) [Search protein sequence]
DTWQDEEYFDSYGTLKLHLEMLADQPRTTKYHSVILQNKESLKDKVILDV
GCGTGIISLFCAHHARPKAVYAVEASDMAQHTSQLVLQNGFADTITVFQQ
KVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDTWLKGDGIIWPTT
AALHLVPCSAEKDYHSKVLFWDNAYEFNLSALKSLAIKEFFSRPKSNHIL
KPEDCLSEPCTILQLDMRTVQVPDLETMRGELRFDIQKAGTLHGFTAWFS
VYFQSLEEGQPQQVLSTGPLHPTTHWKQTLFMMDDPVPVHTGDVVTGSVV
LQRNPVWRRHMSVSLSWVVTSALDPTSQRVGEKVFPIWW
3D structure
PDB5ful Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
ChainA
Resolution1.89 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 SAH A Y114 F115 Y118 M127 R133 G157 C158 I162 E180 A181 K207 V208 E223 M234 S237 Y8 F9 Y12 M21 R27 G51 C52 I56 E74 A75 K101 V102 E117 M128 S131 MOAD: ic50=18.3uM
PDBbind-CN: -logKd/Ki=4.74,IC50=18.3uM
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:5ful, PDBe:5ful, PDBj:5ful
PDBsum5ful
PubMed27879050
UniProtQ3UKX1

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