Structure of PDB 2fyt Chain A

Receptor sequence
>2fytA (length=311) Species: 9606 (Homo sapiens) [Search protein sequence]
FSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILS
MFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPV
EKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAV
SDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIK
HIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFS
TGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLT
LNNSTQTYGLQ
3D structure
PDB2fyt The Crystal Structure of Human HMT1 hnRNP methyltransferase-like 3 in complex with SAH.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D253 E346 E355 H496
Catalytic site (residue number reindexed from 1) D16 E109 E118 H259
Enzyme Commision number 2.1.1.319: type I protein arginine 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 Y241 M250 R256 G280 C281 I285 D302 Q303 K329 I330 E331 M357 S360 Y4 M13 R19 G43 C44 I48 D65 Q66 K92 I93 E94 M120 S123 BindingDB: IC50=2000nM
Gene Ontology
Molecular Function
GO:0016274 protein-arginine N-methyltransferase activity
Biological Process
GO:0018216 peptidyl-arginine methylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2fyt, PDBe:2fyt, PDBj:2fyt
PDBsum2fyt
PubMed
UniProtO60678|ANM3_HUMAN Protein arginine N-methyltransferase 3 (Gene Name=PRMT3)

[Back to BioLiP]