Structure of PDB 6vo5 Chain B

Receptor sequence

>6vo5B (length=318) Species: 9606 (Homo sapiens) [Search protein sequence]

GSKKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAF
GYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPP
GFCTNTNDFLSLLEKEVDFKPFGTLLHTYSVLENFTFQIYKADMTCRGFR
EYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATVGYM
TVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPTVLD
ITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMAIEAQQKFK
INKQHARRVYEILRLLVT

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

Resolution

1.6 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	M241 E276
Catalytic site (residue number reindexed from 1)	M219 E254
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	B	Y55 H57 Q58 D62 E64 E187 T188 S190 W199 Y225 Y227 R237 S239 Q240 E276	Y38 H40 Q41 D45 E47 E165 T166 S168 W177 Y203 Y205 R215 S217 Q218 E254
BS02	CO6	B	M241 L242 I243 Q248 G249 G251 G253 A254 S279 S281 K284 L285 F288	M219 L220 I221 Q226 G227 G229 G231 A232 S257 S259 K262 L263 F266

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

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Molecular Function

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Biological Process

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Cellular Component

External links

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

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