Structure of PDB 3m54 Chain A

Receptor sequence
>3m54A (length=245) Species: 9606 (Homo sapiens) [Search protein sequence]
HGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMI
EGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESER
VYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGN
TLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIFDMFVHPRFGP
IKCIRTLRAVEADEELTVAYGYDHSPPEAPEWYQVELKAFQATQQ
3D structure
PDB3m54 SET7/9 catalytic mutants reveal the role of active site water molecules in lysine multiple methylation.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y245 H293 H297 F305 Y335
Catalytic site (residue number reindexed from 1) Y130 H178 H182 F190 Y220
Enzyme Commision number 2.1.1.364: [histone H3]-lysine(4) N-methyltransferase.
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 A Y245 D256 R258 W260 N263 T266 L267 S268 D270 F305 K317 Y335 Y337 D338 E348 Y130 D141 R143 W145 N148 T151 L152 S153 D155 F190 K202 Y220 Y222 D223 E228
BS02 SAH A A226 E228 H293 K294 N296 H297 Y335 W352 A111 E113 H178 K179 N181 H182 Y220 W232 BindingDB: IC50=30000nM
Gene Ontology
Molecular Function
GO:0016279 protein-lysine N-methyltransferase activity
GO:0140945 histone H3K4 monomethyltransferase activity
Biological Process
GO:0006355 regulation of DNA-templated transcription
Cellular Component
GO:0005694 chromosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3m54, PDBe:3m54, PDBj:3m54
PDBsum3m54
PubMed20675860
UniProtQ8WTS6|SETD7_HUMAN Histone-lysine N-methyltransferase SETD7 (Gene Name=SETD7)

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