Structure of PDB 4ypa Chain B

Receptor sequence
>4ypaB (length=212) Species: 9606 (Homo sapiens) [Search protein sequence]
YKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFAECS
PNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIE
YLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINH
SCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKAQLC
KCGFEKCRGIIG
3D structure
PDB4ypa Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y2169 Y2255
Catalytic site (residue number reindexed from 1) Y101 Y187
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 B C2093 C2104 C2108 C25 C36 C40
BS02 ZN B C2104 C2117 C2122 C2128 C36 C49 C54 C60
BS03 ZN B C2220 C2268 C2270 C2275 C152 C200 C202 C207
BS04 SAM B K2150 W2152 H2193 Y2194 R2214 N2217 H2218 Y2255 Q2266 C2268 K2269 I2279 K82 W84 H125 Y126 R146 N149 H150 Y187 Q198 C200 K201 I211
Gene Ontology
Molecular Function
GO:0042054 histone methyltransferase activity
Cellular Component
GO:0005634 nucleus

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Molecular Function
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Cellular Component
External links
PDB RCSB:4ypa, PDBe:4ypa, PDBj:4ypa
PDBsum4ypa
PubMed26292256
UniProtQ9NR48|ASH1L_HUMAN Histone-lysine N-methyltransferase ASH1L (Gene Name=ASH1L)

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