Structure of PDB 6vo5 Chain A

Receptor sequence

>6vo5A (length=322) Species: 9606 (Homo sapiens)

KKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGY
KGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGF
CTNTNDFLSLLEKEVDFKPFGTLLHTYSVLSPTGGENFTFQIYKADMTCR
GFREYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATV
GYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPT
VLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMAIEAQQ
KFKINKQHARRVYEILRLLVTD

3D structure

• PDB: 6vo5 Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4
• Chain: A
• Resolution: 1.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): M241 E276
• Catalytic site (residue number reindexed from 1): M222 E257
• Enzyme Commision number: 2.3.1.48: histone acetyltransferase.

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	peptide	A	Y55 H57 Q58 D62 E64 E187 T188 S190 W199 Y225 R237 S239 Q240 E276	Y36 H38 Q39 D43 E45 E168 T169 S171 W180 Y206 R218 S220 Q221 E257
BS02	CO6	A	V238 M241 L242 I243 Q248 G249 G251 G253 A254 P278 S279 S281 Y282 K284 L285 F288	V219 M222 L223 I224 Q229 G230 G232 G234 A235 P259 S260 S262 Y263 K265 L266 F269

Gene Ontology

Molecular Function

• GO:0004402 histone acetyltransferase activity
• GO:0042393 histone binding

Biological Process

• GO:0006325 chromatin organization
• GO:0031509 subtelomeric heterochromatin formation

Cellular Component

• GO:0005634 nucleus

External links

• PDB: RCSB:6vo5, PDBe:6vo5, PDBj:6vo5
• PDBsum: 6vo5
• UniProt: O14929|HAT1_HUMAN Histone acetyltransferase type B catalytic subunit (Gene Name=HAT1)