Structure of PDB 7lms Chain A Binding Site BS01

Receptor Information
>7lms Chain A (length=474) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PKEILNLTSELLQKCSSPAPGPGKEWEEYVQIRTLVEKIRKKQKGLSVTF
DGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFL
WVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNIALAFHLLCERASPNSF
WQPYIQTLPSEYDTPLYFEEDEVRYLQSTQAIHDVFSQYKNTARQYAYFY
KVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALI
PLWDMCNHTNGLITTGYNLEDDRCECVALQDFRAGEQIYIFYGTRSNAEF
VIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALH
FTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSWD
NEVKLWTFLEDRASLLLKTYKTTIEEDKSVLKNHDLSVRAKMAIKLRLGE
KEILEKAVKSAAVNREYYRQQMEE
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 chain7lms Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7lms Structure-function analysis of enterovirus protease 2A in complex with its essential host factor SETD3.
Resolution3.5 Å
Binding residue
(original residue number in PDB)		R75 E104 F106 R254 D275 N278 H279 Y313 S325 F327
Binding residue
(residue number reindexed from 1)		R54 E83 F85 R233 D254 N257 H258 Y292 S304 F306
Annotation score5
Enzymatic activity
Enzyme Commision number 2.1.1.85: protein-histidine N-methyltransferase.
Gene Ontology
Molecular Function
GO:0003713 transcription coactivator activity
GO:0003779 actin binding
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0008170 N-methyltransferase activity
GO:0008276 protein methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0016279 protein-lysine N-methyltransferase activity
GO:0018064 protein-L-histidine N-tele-methyltransferase activity
GO:0042800 histone H3K4 methyltransferase activity
GO:0046975 histone H3K36 methyltransferase activity
GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Biological Process
GO:0006338 chromatin remodeling
GO:0018021 peptidyl-histidine methylation
GO:0018023 peptidyl-lysine trimethylation
GO:0030047 actin modification
GO:0032259 methylation
GO:0045893 positive regulation of DNA-templated transcription
GO:0045944 positive regulation of transcription by RNA polymerase II
GO:0051149 positive regulation of muscle cell differentiation
GO:0070472 regulation of uterine smooth muscle contraction
Cellular Component
GO:0000785 chromatin
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7lms, PDBe:7lms, PDBj:7lms
PDBsum7lms
PubMed36075902
UniProtQ86TU7|SETD3_HUMAN Actin-histidine N-methyltransferase (Gene Name=SETD3)

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