1MJA

Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A

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	19
Details	BINDING SITE FOR RESIDUE COA A 500

Chain	Residue
A	TRP180
A	MET314
A	GLY315
A	GLY317
A	LYS318
A	LEU341
A	SER342
A	SER348
A	ARG421
A	HOH504
A	HOH505
A	PHE258
A	LEU259
A	SCY304
A	ILE305
A	LEU306
A	THR307
A	GLN312
A	ARG313

---

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

---

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

---

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	SCY304

---

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

Chain	Residue	Details
A	LYS262

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 525

Chain	Residue	Details
A	SCY304	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLU338	activator, proton acceptor, proton donor

---