Structure of PDB 4j83 Chain A

Receptor sequence
>4j83A (length=242) Species: 9606 (Homo sapiens) [Search protein sequence]
GVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIE
GKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERV
YVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNT
LSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPI
KCIRTLRAVEADEELTVAYGYDHSPPEAPEWYQVELKAFQAT
3D structure
PDB4j83 Conservation and functional importance of carbon-oxygen hydrogen bonding in AdoMet-dependent methyltransferases.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 V255 D256 R258 W260 N263 T266 L267 S268 Y305 K317 Y335 Y337 V139 D140 R142 W144 N147 T150 L151 S152 Y189 K201 Y219 Y221
BS02 SAM A A226 E228 G264 N265 H293 K294 N296 H297 Y335 W352 A110 E112 G148 N149 H177 K178 N180 H181 Y219 W231
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4j83, PDBe:4j83, PDBj:4j83
PDBsum4j83
PubMed24093804
UniProtQ8WTS6|SETD7_HUMAN Histone-lysine N-methyltransferase SETD7 (Gene Name=SETD7)

[Back to BioLiP]