6V8N

Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 17

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	3
Details	binding site for residue SO4 A 1701

Chain	Residue
A	ARG1478
A	ARG1478
A	HIS1481

---

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 1702

Chain	Residue
A	ALA1350
A	GLU1351
A	SER1352
A	ARG1462

---

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 1703

Chain	Residue
A	HOH1814
A	LEU1398
A	LYS1558

---

site_id	AC4
Number of Residues	10
Details	binding site for residue QS1 A 1704

Chain	Residue
A	LEU1398
A	ASP1399
A	SER1400
A	GLY1443
A	ASP1444
A	HIS1451
A	GLN1455
A	ILE1457
A	LEU1463
A	TRP1466

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Region: {"description":"Interaction with histone","evidences":[{"source":"PubMed","id":"18273021","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24819397","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17065153","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"15004546","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---