9FKR

KAT6A IN COMPLEX WITH SMALL MOLECULE INHIBITOR BAY-184

This is a non-PDB format compatible entry.

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
B	0004402	molecular_function	histone acetyltransferase activity
B	0006355	biological_process	regulation of DNA-templated transcription

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	50
Details	Zinc finger: {"description":"C2HC MYST-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]}

Chain

Residue

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q9H7Z6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

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site_id	SWS_FT_FI3
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

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