Structure of PDB 3os5 Chain A

Receptor sequence
>3os5A (length=249) Species: 9606 (Homo sapiens) [Search protein sequence]
HGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMI
EGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESER
VYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGN
TLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGP
IKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQ
3D structure
PDB3os5 A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability.
ChainA
Resolution1.69 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 Y245 D256 R258 W260 N263 T266 L267 S268 Y305 Y335 G336 Y337 P341 K344 E348 Y130 D141 R143 W145 N148 T151 L152 S153 Y190 Y220 G221 Y222 P226 K229 E233
BS02 SAH A A226 E228 H293 K294 N296 H297 Y335 W352 E356 A111 E113 H178 K179 N181 H182 Y220 W237 E241
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:3os5, PDBe:3os5, PDBj:3os5
PDBsum3os5
PubMed21151116
UniProtQ8WTS6|SETD7_HUMAN Histone-lysine N-methyltransferase SETD7 (Gene Name=SETD7)

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