Structure of PDB 5fub Chain A Binding Site BS01

Receptor Information
>5fub Chain A (length=337) Species: 7955 (Danio rerio) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GDAWQDDEYFGNYGTLRLHLEMLSDKPRTETYRQVILSNSAALREKVVLD
LGCGTGVISLFCALLAKPAGVYAVEASSMAEHTEELVKQNGCDGVVTVFQ
ERAENLTLPTKVDVLVSEWMGNCLLFEYMLESVLLARDRWLKKGGMMWPS
SACLTIVPCQAFSDYRQKVEFWENPYGLNFSYLQSLAQKEFLSKPKFSHH
LQPEDCLSTPADVITLDMVTIQVSDLERLKGEFTFTVEKSGMFHGFTVWF
SAHFQCLEEDGPSIELNTGPYSEITHWKQTLFMLDAPVSVEEGDIIAGSI
RLQRNPIWRRHLSITFLWNINSTEVSTVKTKCFPMWR
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 chain5fub Chain A Residue 409 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5fub Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
Resolution1.997 Å
Binding residue
(original residue number in PDB)		Y80 F81 Y84 M93 R99 G123 C124 V128 E146 A147 R173 M200 S203
Binding residue
(residue number reindexed from 1)		Y9 F10 Y13 M22 R28 G52 C53 V57 E75 A76 R102 M129 S132
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D96 E189 E198 H347
Catalytic site (residue number reindexed from 1) D25 E118 E127 H276
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.
Gene Ontology
Molecular Function
GO:0016274 protein-arginine N-methyltransferase activity
Biological Process
GO:0018216 peptidyl-arginine methylation

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:5fub, PDBe:5fub, PDBj:5fub
PDBsum5fub
PubMed27879050
UniProtA1L1Q4

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