Structure of PDB 5v21 Chain A Binding Site BS04

Receptor Information
>5v21 Chain A (length=245) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PSCVMDDFRDPQRWKECAKQGKMPCYFDLIEENVYLTERQCECTPLSKDE
RAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTE
KKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMA
LKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPS
GSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGK
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5v21 Chain A Residue 1803 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5v21 Molecular basis for the role of oncogenic histone mutations in modulating H3K36 methylation.
Resolution2.415 Å
Binding residue
(original residue number in PDB)		C1631 C1678 C1680 C1685
Binding residue
(residue number reindexed from 1)		C173 C220 C222 C227
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y1579 Y1666
Catalytic site (residue number reindexed from 1) Y121 Y208
Enzyme Commision number 2.1.1.-
2.1.1.359: [histone H3]-lysine(36) N-trimethyltransferase.
Gene Ontology
Molecular Function
GO:0016279 protein-lysine N-methyltransferase activity
GO:0042054 histone methyltransferase activity
GO:0046975 histone H3K36 methyltransferase activity
Cellular Component
GO:0005634 nucleus

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Molecular Function
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Cellular Component
External links
PDB RCSB:5v21, PDBe:5v21, PDBj:5v21
PDBsum5v21
PubMed28256625
UniProtQ9BYW2|SETD2_HUMAN Histone-lysine N-methyltransferase SETD2 (Gene Name=SETD2)

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