Structure of PDB 4ype Chain A

Receptor sequence

>4ypeA (length=217) Species: 9606 (Homo sapiens)

AMAGSYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMI
FAECSPNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAG
QFIIEYLGEVVSEQEFRNRMIEQYHNHSDFYCLNLDSGMVIDSYRMGNEA
RFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVE
KQQLCKCGFEKCRGIIG

3D structure

• PDB: 4ype Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y2169 Y2255
• Catalytic site (residue number reindexed from 1): Y106 Y192
• Enzyme Commision number: 2.1.1.359: [histone H3]-lysine(36) N-trimethyltransferase.
  2.1.1.367: [histone H3]-lysine(9) 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	ZN	A	C2220 C2268 C2270 C2275	C157 C205 C207 C212
BS02	ZN	A	C2104 C2117 C2122 C2128	C41 C54 C59 C65
BS03	ZN	A	C2091 C2093 C2104 C2108	C28 C30 C41 C45
BS04	SAM	A	K2150 W2152 D2192 F2193 Y2194 R2214 F2215 N2217 H2218 Y2255 Q2266 C2268 K2269 I2279	K87 W89 D129 F130 Y131 R151 F152 N154 H155 Y192 Q203 C205 K206 I216

Gene Ontology

Molecular Function

• GO:0042054 histone methyltransferase activity

Cellular Component

• GO:0005634 nucleus

External links

• PDB: RCSB:4ype, PDBe:4ype, PDBj:4ype
• PDBsum: 4ype
• PubMed: 26292256
• UniProt: Q9NR48|ASH1L_HUMAN Histone-lysine N-methyltransferase ASH1L (Gene Name=ASH1L)