Structure of PDB 1o9s Chain A

Receptor sequence
>1o9sA (length=250) Species: 9606 (Homo sapiens) [Search protein sequence]
GVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIE
GKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERV
YVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNT
LSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPI
KCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK
3D structure
PDB1o9s Structure and Catalytic Mechanism of the Human Histone Methyltransferase Set7/9
ChainA
Resolution1.75 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) Y129 H177 H181 Y189 Y219
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 V255 D256 R258 W260 N263 G264 T266 L267 S268 Y305 K317 Y335 Y337 Y129 V139 D140 R142 W144 N147 G148 T150 L151 S152 Y189 K201 Y219 Y221
BS02 SAH A A226 E228 H293 N296 H297 Y335 W352 E356 A110 E112 H177 N180 H181 Y219 W236 E240
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:1o9s, PDBe:1o9s, PDBj:1o9s
PDBsum1o9s
PubMed12540855
UniProtQ8WTS6|SETD7_HUMAN Histone-lysine N-methyltransferase SETD7 (Gene Name=SETD7)

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