6K4N

Cryo-EM structure of p300

Replaces:  5XZS

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 PROSITE/UniProt

site_id	PS00633
Number of Residues	60
Details	BROMODOMAIN_1 Bromodomain signature. SlpFrqpvDpqllgipDYFdiVkspMdlstIkrkldtgq..Yqepwqyvddiwl.MfnNAwlY

Chain	Residue	Details
A	SER1072-TYR1131

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	107
Details	Domain: {"description":"Bromo","evidences":[{"source":"PROSITE-ProRule","id":"PRU00035","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Region: {"description":"Interaction with histone","evidences":[{"source":"PubMed","id":"18273021","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24819397","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"B2RWS6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17065153","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
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_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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