6V8B

Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 1

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	13
Details	binding site for residue QRY A 1701

Chain	Residue
A	LEU1398
A	PRO1458
A	ARG1462
A	LEU1463
A	TRP1466
A	ASP1399
A	SER1400
A	CYS1438
A	PRO1440
A	TYR1446
A	HIS1451
A	GLN1455
A	ILE1457

---

site_id	AC2
Number of Residues	1
Details	binding site for residue CL A 1702

Chain	Residue
A	LEU1398

---

site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 1703

Chain	Residue
A	THR1357
A	GLY1626

---

site_id	AC4
Number of Residues	6
Details	binding site for residue SO4 A 1704

Chain	Residue
A	LEU1293
A	VAL1326
A	ILE1619
A	CYS1621
A	LEU1658
A	SER1662

---

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	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---