Structure of PDB 4ynm Chain A

Receptor sequence

>4ynmA (length=215) Species: 9606 (Homo sapiens)

AGSYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFA
ECSPNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQF
IIEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARF
INHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQ
QLCKCGFEKCRGIIG

3D structure

• PDB: 4ynm Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.
• Chain: A
• Resolution: 2.19 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y2169 Y2255
• Catalytic site (residue number reindexed from 1): Y104 Y190
• 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	C155 C203 C205 C210
BS02	ZN	A	C2104 C2117 C2122 C2128	C39 C52 C57 C63
BS03	ZN	A	C2091 C2093 C2104 C2108	C26 C28 C39 C43
BS04	SAM	A	K2150 G2151 W2152 D2192 H2193 Y2194 R2214 F2215 N2217 H2218 Y2255 Q2266 L2267 C2268 K2269 I2279	K85 G86 W87 D127 H128 Y129 R149 F150 N152 H153 Y190 Q201 L202 C203 K204 I214

Gene Ontology

Molecular Function

• GO:0042054 histone methyltransferase activity

Cellular Component

• GO:0005634 nucleus

External links

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