Structure of PDB 4ypu Chain A

Receptor sequence
>4ypuA (length=214) Species: 9606 (Homo sapiens) [Search protein sequence]
GSYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFAE
CSPNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFI
IEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFI
NHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVELQQ
LCKCGFEKCRGIIG
3D structure
PDB4ypu Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.
ChainA
Resolution2.6 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) Y103 Y189
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 C154 C202 C204 C209
BS02 ZN A C2104 C2117 C2128 C38 C51 C62
BS03 ZN A C2091 C2093 C2104 C2108 C25 C27 C38 C42
BS04 SAM A K2150 W2152 D2192 H2193 Y2194 R2214 F2215 N2217 H2218 Y2255 Q2266 K2269 K84 W86 D126 H127 Y128 R148 F149 N151 H152 Y189 Q200 K203
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:4ypu, PDBe:4ypu, PDBj:4ypu
PDBsum4ypu
PubMed26292256
UniProtQ9NR48|ASH1L_HUMAN Histone-lysine N-methyltransferase ASH1L (Gene Name=ASH1L)

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