Structure of PDB 1peg Chain B

Receptor sequence
>1pegB (length=256) Species: 5141 (Neurospora crassa) [Search protein sequence]
LPISIVNREDDAFLNPNFRFIDHSIIGKNVPVADQSFRVGCSCASDEECM
YSTCQCLDEMAPKRFAYYSQGAKKGLLRDRVLQSQEPIYECHQGCACSKD
CPNRVVERGRTVPLQIFRTKDRGWGVKCPVNIKRGQFVDRYLGEIITSEE
ADRRRAESTIARRKDVYLFALDKFSDPDSLLEVDGEYMSGPTRFINHSCD
PNMAIFARVGDHADKHIHDLALFAIKDIPKGTELTFDYVNGTKCLCGTAK
CRGYLW
3D structure
PDB1peg Structural basis for the product specificity of histone lysine methyltransferases
ChainB
Resolution2.59 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y178 Y283
Catalytic site (residue number reindexed from 1) Y141 Y238
Enzyme Commision number 2.1.1.355: [histone H3]-lysine(9) N-trimethyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide B Y178 V203 L205 F206 A207 D209 I250 Y283 W318 Y141 V166 L168 F169 A170 D172 I205 Y238 W256
BS02 ZN B C244 C306 C308 C313 C199 C244 C246 C251
BS03 SAH B W161 V203 Y204 N241 H242 C306 L317 W124 V166 Y167 N196 H197 C244 L255
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

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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)

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