Structure of PDB 1peg Chain A

Receptor sequence
>1pegA (length=266) Species: 5141 (Neurospora crassa) [Search protein sequence]
LPISIVNREDDAFLNPNFRFIDHSIIGKNVPVADQSFRVGCSCASDEECM
YSTCQCLDEMAPDPYTRKKRFAYYSQGAKKGLLRDRVLQSQEPIYECHQG
CACSKDCPNRVVERGRTVPLQIFRTKDRGWGVKCPVNIKRGQFVDRYLGE
IITSEEADRRRAESTIARRKDVYLFALDKFSDPDSLDPLLAGPLEVDGEY
MSGPTRFINHSCDPNMAIFARVGDHADKHIHDLALFAIKDIPKGTELTFD
YVNCLCGTAKCRGYLW
3D structure
PDB1peg Structural basis for the product specificity of histone lysine methyltransferases
ChainA
Resolution2.59 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 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.
Interaction with ligand
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1peg, PDBe:1peg, PDBj:1peg
PDBsum1peg
PubMed12887903
UniProtQ8X225|DIM5_NEUCR Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (Gene Name=dim-5)

[Back to BioLiP]