Structure of PDB 3m53 Chain A

Receptor sequence
>3m53A (length=246) Species: 9606 (Homo sapiens) [Search protein sequence]
HGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMI
EGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESER
VYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGN
TLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGP
IKCIRTLRAVEADEELTVAYGYDHSPGPEAPEWYQVELKAFQATQQ
3D structure
PDB3m53 SET7/9 catalytic mutants reveal the role of active site water molecules in lysine multiple methylation.
ChainA
Resolution1.85 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 Y305 Y335
Catalytic site (residue number reindexed from 1) Y130 H178 H182 Y190 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 H252 D256 R258 W260 N263 T266 L267 S268 E271 Y305 K317 Y335 Y337 D338 H137 D141 R143 W145 N148 T151 L152 S153 E156 Y190 K202 Y220 Y222 D223
BS02 SAH A A226 E228 H293 K294 N296 H297 Y335 W352 A111 E113 H178 K179 N181 H182 Y220 W233
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:3m53, PDBe:3m53, PDBj:3m53
PDBsum3m53
PubMed20675860
UniProtQ8WTS6|SETD7_HUMAN Histone-lysine N-methyltransferase SETD7 (Gene Name=SETD7)

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