3TO7

Crystal structure of yeast Esa1 HAT domain bound to coenzyme A with active site lysine acetylated

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004402	molecular_function	histone acetyltransferase activity
A	0006355	biological_process	regulation of DNA-templated transcription

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE COA A 500

Chain	Residue
A	HOH3
A	GLN312
A	ARG313
A	MET314
A	GLY315
A	GLY317
A	LYS318
A	SER342
A	SER348
A	ARG421
A	HOH464
A	HOH4
A	HOH470
A	HOH44
A	PHE258
A	LEU259
A	CYS304
A	ILE305
A	LEU306
A	THR307

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CAD A 501

Chain	Residue
A	ALY262
A	THR263
A	HOH466

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site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 502

Chain	Residue
A	HOH66
A	HOH114
A	HOH137
A	ARG165
A	ASN166
A	LEU167
A	GLU188
A	LEU189
A	THR190
A	GLU192
A	PHE194

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site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	HOH75
A	PHE182
A	TYR185
A	ILE187
A	LEU189
A	GLN312
A	ARG313

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 504

Chain	Residue
A	ARG230
A	HIS284
A	TYR397
A	LYS398

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	25
Details	ZN_FING: C2HC MYST-type; degenerate => ECO:0000255|PROSITE-ProRule:PRU01063

Chain	Residue	Details
A	ILE195-LEU220

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000303|PubMed:12368900, ECO:0000303|PubMed:17223684, ECO:0000303|PubMed:18245364, ECO:0000303|PubMed:22020126, ECO:0000305

Chain	Residue	Details
A	GLU338

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:11106757, ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126

Chain	Residue	Details
A	ALA303
A	GLN312
A	SER342

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Important for catalytic activity => ECO:0000305

Chain	Residue	Details
A	CYS304

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:22020126

Chain	Residue	Details
A	ALY262

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 525

Chain	Residue	Details
A	CYS304	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLU338	activator, proton acceptor, proton donor

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