2ZFN

Self-acetylation mediated histone H3 lysine 56 acetylation by rtt109

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000785	cellular_component	chromatin
A	0004402	molecular_function	histone acetyltransferase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0006325	biological_process	chromatin organization
A	0006334	biological_process	nucleosome assembly
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006974	biological_process	DNA damage response
A	0010468	biological_process	regulation of gene expression
A	0010484	molecular_function	histone H3 acetyltransferase activity
A	0010526	biological_process	retrotransposon silencing
A	0016740	molecular_function	transferase activity
A	0032931	molecular_function	histone H3K56 acetyltransferase activity
A	0036211	biological_process	protein modification process
A	0036408	molecular_function	histone H3K14 acetyltransferase activity
A	0043007	biological_process	maintenance of rDNA
A	0043992	molecular_function	histone H3K9 acetyltransferase activity
A	0043994	molecular_function	histone H3K23 acetyltransferase activity
A	0044017	molecular_function	histone H3K27 acetyltransferase activity
A	0061733	molecular_function	peptide-lysine-N-acetyltransferase activity
A	0070775	cellular_component	H3 histone acetyltransferase complex
A	1990414	biological_process	replication-born double-strand break repair via sister chromatid exchange
A	2001032	biological_process	regulation of double-strand break repair via nonhomologous end joining

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ACO A 500

Chain	Residue
A	SER86
A	ALA196
A	TYR199
A	LYS210
A	HIS211
A	ILE212
A	LEU213
A	LEU218
A	TRP221
A	TRP222
A	THR271
A	LYS87
A	SER272
A	HOH803
A	HOH851
A	HOH867
A	HOH901
A	ALA88
A	ASP89
A	THR90
A	ARG101
A	PHE192
A	ARG194
A	PRO195

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 601

Chain	Residue
A	SER86
A	LYS87
A	PHE192
A	TYR199
A	ASP287
A	PRO289

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18707894

Chain	Residue	Details
A	ASP288

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:2ZFN, ECO:0007744|PDB:3CZ7, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0

Chain	Residue	Details
A	ARG97
A	HIS211
A	ALA88

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0007744|PDB:3QM0

Chain	Residue	Details
A	PHE192

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0

Chain	Residue	Details
A	ALA196

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:2ZFN, ECO:0007744|PDB:3CZ7, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35

Chain	Residue	Details
A	TRP221

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104

Chain	Residue	Details
A	ALY290

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