Structure of PDB 1n6c Chain A

Receptor sequence
>1n6cA (length=283) Species: 9606 (Homo sapiens) [Search protein sequence]
GGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCWIYYPDGGS
LVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEG
RPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGE
GLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVP
EPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEAD
EELTVAYGYSPPGKSGPEAPEWYQVELKAFQAT
3D structure
PDB1n6c Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet
ChainA
Resolution2.3 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) Y167 H215 H219 Y227 Y257
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 SAM A A226 E228 G264 N265 H293 K294 A295 N296 H297 Y335 W352 E356 A148 E150 G186 N187 H215 K216 A217 N218 H219 Y257 W272 E276
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:1n6c, PDBe:1n6c, PDBj:1n6c
PDBsum1n6c
PubMed12514135
UniProtQ8WTS6|SETD7_HUMAN Histone-lysine N-methyltransferase SETD7 (Gene Name=SETD7)

[Back to BioLiP]