Structure of PDB 1peg Chain A Binding Site BS04

Receptor Information

>1peg Chain A (length=266) Species: 5141 (Neurospora crassa)

LPISIVNREDDAFLNPNFRFIDHSIIGKNVPVADQSFRVGCSCASDEECM
YSTCQCLDEMAPDPYTRKKRFAYYSQGAKKGLLRDRVLQSQEPIYECHQG
CACSKDCPNRVVERGRTVPLQIFRTKDRGWGVKCPVNIKRGQFVDRYLGE
IITSEEADRRRAESTIARRKDVYLFALDKFSDPDSLDPLLAGPLEVDGEY
MSGPTRFINHSCDPNMAIFARVGDHADKHIHDLALFAIKDIPKGTELTFD
YVNCLCGTAKCRGYLW

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 1peg Chain A Residue 3

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1peg Structural basis for the product specificity of histone lysine methyltransferases
• Resolution: 2.59 Å
• Binding residue (original residue number in PDB): C66 C68 C74 C79
• Binding residue (residue number reindexed from 1): C41 C43 C49 C54
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): Y178 Y283
• Catalytic site (residue number reindexed from 1): Y147 Y251
• Enzyme Commision number: 2.1.1.355: [histone H3]-lysine(9) N-trimethyltransferase.

Gene Ontology

Molecular Function

• GO:0003690 double-stranded DNA binding
• GO:0005515 protein binding
• GO:0008168 methyltransferase activity
• GO:0008270 zinc ion binding
• GO:0042054 histone methyltransferase activity
• GO:0046872 metal ion binding
• GO:0046974 histone H3K9 methyltransferase activity
• GO:0140949 histone H3K9 trimethyltransferase activity

Biological Process

• GO:0006338 chromatin remodeling
• GO:0032259 methylation

Cellular Component

• GO:0005634 nucleus
• GO:0005694 chromosome

External links

• PDB: RCSB:1peg, PDBe:1peg, PDBj:1peg
• PDBsum: 1peg
• PubMed: 12887903
• UniProt: Q8X225|DIM5_NEUCR Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (Gene Name=dim-5)