Structure of PDB 2fyt Chain A Binding Site BS01

Receptor Information
>2fyt Chain A (length=311) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILS
MFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPV
EKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAV
SDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIK
HIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFS
TGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLT
LNNSTQTYGLQ
Ligand information
Ligand IDSAH
InChIInChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
InChIKeyZJUKTBDSGOFHSH-WFMPWKQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CCSC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23)C(O)=O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CSCCC(C(=O)O)N)O)O)N
CACTVS 3.341N[C@@H](CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCSCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CSCC[C@@H](C(=O)O)N)O)O)N
FormulaC14 H20 N6 O5 S
NameS-ADENOSYL-L-HOMOCYSTEINE
ChEMBLCHEMBL418052
DrugBankDB01752
ZINCZINC000004228232
PDB chain2fyt Chain A Residue 549 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fyt The Crystal Structure of Human HMT1 hnRNP methyltransferase-like 3 in complex with SAH.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		Y241 M250 R256 G280 C281 I285 D302 Q303 K329 I330 E331 M357 S360
Binding residue
(residue number reindexed from 1)		Y4 M13 R19 G43 C44 I48 D65 Q66 K92 I93 E94 M120 S123
Annotation score5
Binding affinityBindingDB: IC50=2000nM
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.
Gene Ontology
Molecular Function
GO:0016274 protein-arginine N-methyltransferase activity
Biological Process
GO:0018216 peptidyl-arginine methylation

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

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