Structure of PDB 5fqn Chain A Binding Site BS01
Receptor Information
>5fqn Chain A (length=322) Species:
10090
(Mus musculus) [
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LYYECDVSVHEEMIADQVRTEAYRLGILKNWAALRGKTVLDVGAGTGILS
IFCAQAGARRVYAVEASAIWQQAREVVRLNGLEDRVHVLPGPVETVELPE
RVDAIVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFVAPIS
DQMLEWRLGFWSQVKQHYGVDMSCMESFATRCLMGHSEIVVQDLSGEDVL
ARPQRFAQLELARAGLEQELEAGVGGRFRCSCYGSAPLHGFAVWFQVTFP
GPLVLSTSPLHPATHWKQALLYLNEPVPVEQDTDISGEITLLPSPDNPRR
LRILLRYKVGDHEEKTKDFAME
Ligand information
Ligand ID
SAH
InChI
InChI=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
InChIKey
ZJUKTBDSGOFHSH-WFMPWKQPSA-N
SMILES
Software
SMILES
CACTVS 3.341
N[CH](CCSC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23)C(O)=O
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CSCCC(C(=O)O)N)O)O)N
CACTVS 3.341
N[C@@H](CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23)C(O)=O
ACDLabs 10.04
O=C(O)C(N)CCSCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CSCC[C@@H](C(=O)O)N)O)O)N
Formula
C14 H20 N6 O5 S
Name
S-ADENOSYL-L-HOMOCYSTEINE
ChEMBL
CHEMBL418052
DrugBank
DB01752
ZINC
ZINC000004228232
PDB chain
5fqn Chain A Residue 1378 [
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Receptor-Ligand Complex Structure
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PDB
5fqn
Crystal Strcutures of Prmt6 in Complex with Sah in Alternative Conformations
Resolution
1.657 Å
Binding residue
(original residue number in PDB)
M63 R69 G93 A94 L99 E115 A116 P142 V143 E144 E158 M169 S172
Binding residue
(residue number reindexed from 1)
M13 R19 G43 A44 L49 E65 A66 P92 V93 E94 E108 M119 S122
Annotation score
5
Enzymatic activity
Catalytic site (original residue number in PDB)
D66 E158 E167 H320
Catalytic site (residue number reindexed from 1)
D16 E108 E117 H265
Enzyme Commision number
2.1.1.319
: type I protein arginine methyltransferase.
Gene Ontology
Molecular Function
GO:0003682
chromatin binding
GO:0005515
protein binding
GO:0008168
methyltransferase activity
GO:0008469
histone arginine N-methyltransferase activity
GO:0016274
protein-arginine N-methyltransferase activity
GO:0035241
protein-arginine omega-N monomethyltransferase activity
GO:0035242
protein-arginine omega-N asymmetric methyltransferase activity
GO:0042054
histone methyltransferase activity
GO:0042393
histone binding
GO:0044020
histone H4R3 methyltransferase activity
GO:0070611
histone H3R2 methyltransferase activity
GO:0070612
histone H2AR3 methyltransferase activity
Biological Process
GO:0000122
negative regulation of transcription by RNA polymerase II
GO:0006281
DNA repair
GO:0006325
chromatin organization
GO:0006338
chromatin remodeling
GO:0010821
regulation of mitochondrion organization
GO:0018216
peptidyl-arginine methylation
GO:0032259
methylation
GO:0036211
protein modification process
GO:0045892
negative regulation of DNA-templated transcription
GO:0090398
cellular senescence
GO:1901796
regulation of signal transduction by p53 class mediator
GO:2000059
negative regulation of ubiquitin-dependent protein catabolic process
Cellular Component
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005730
nucleolus
View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:5fqn
,
PDBe:5fqn
,
PDBj:5fqn
PDBsum
5fqn
PubMed
UniProt
Q6NZB1
|ANM6_MOUSE Protein arginine N-methyltransferase 6 (Gene Name=Prmt6)
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