Structure of PDB 5dx0 Chain B Binding Site BS02
Receptor Information
>5dx0 Chain B (length=343) Species:
9606
(Homo sapiens) [
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SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
Ligand information
Ligand ID
SFG
InChI
InChI=1S/C15H23N7O5/c16-6(1-2-7(17)15(25)26)3-8-10(23)11(24)14(27-8)22-5-21-9-12(18)19-4-20-13(9)22/h4-8,10-11,14,23-24H,1-3,16-17H2,(H,25,26)(H2,18,19,20)/t6-,7-,8+,10+,11+,14+/m0/s1
InChIKey
LMXOHSDXUQEUSF-YECHIGJVSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.7.0
c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)C[C@H](CC[C@@H](C(=O)O)N)N)O)O)N
OpenEye OEToolkits 1.7.0
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CC(CCC(C(=O)O)N)N)O)O)N
CACTVS 3.370
N[CH](CC[CH](N)C(O)=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
CACTVS 3.370
N[C@@H](CC[C@H](N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
ACDLabs 12.01
O=C(O)C(N)CCC(N)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
Formula
C15 H23 N7 O5
Name
SINEFUNGIN;
ADENOSYL-ORNITHINE
ChEMBL
CHEMBL1214186
DrugBank
DB01910
ZINC
ZINC000004217451
PDB chain
5dx0 Chain B Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
5dx0
Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
Resolution
2.05 Å
Binding residue
(original residue number in PDB)
Y149 F150 Y153 Q159 M162 R168 G192 C193 I197 L198 E214 A215 K241 V242 E243 E257 M268
Binding residue
(residue number reindexed from 1)
Y15 F16 Y19 Q25 M28 R34 G58 C59 I63 L64 E80 A81 K107 V108 E109 E123 M134
Annotation score
3
Enzymatic activity
Catalytic site (original residue number in PDB)
D165 E257 E266 H414
Catalytic site (residue number reindexed from 1)
D31 E123 E132 H280
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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:5dx0
,
PDBe:5dx0
,
PDBj:5dx0
PDBsum
5dx0
PubMed
26551522
UniProt
Q86X55
|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)
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