6BA4

Crystal structure of MYST acetyltransferase domain in complex with Acetyl-CoA cofactor

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	4
Details	binding site for residue ZN A 801

Chain	Residue
A	CYS540
A	CYS543
A	HIS556
A	CYS560

---

site_id	AC2
Number of Residues	4
Details	binding site for residue NA A 802

Chain	Residue
A	ASP520
A	NA803
A	NA804
A	HOH1028

---

site_id	AC3
Number of Residues	4
Details	binding site for residue NA A 803

Chain	Residue
A	TRP522
A	TYR549
A	NA802
A	ASP520

---

site_id	AC4
Number of Residues	5
Details	binding site for residue NA A 804

Chain	Residue
A	ASP520
A	MET547
A	LYS548
A	SER552
A	NA802

---

site_id	AC5
Number of Residues	23
Details	binding site for residue ACO A 805

Chain	Residue
A	PHE600
A	LEU601
A	SER645
A	CYS646
A	ILE647
A	MET648
A	ILE649
A	GLN654
A	ARG655
A	ARG656
A	GLY657
A	GLY659
A	ARG660
A	GLU680
A	SER684
A	LEU686
A	SER690
A	SER693
A	GLN760
A	7L1806
A	HOH901
A	HOH902
A	HOH907

---

site_id	AC6
Number of Residues	27
Details	binding site for residue 7L1 A 806

Chain	Residue
A	PHE600
A	LEU601
A	SER645
A	CYS646
A	ILE647
A	MET648
A	ILE649
A	GLN654
A	ARG655
A	ARG656
A	GLY657
A	GLY659
A	ARG660
A	PRO679
A	GLU680
A	LEU683
A	SER684
A	LEU686
A	GLY687
A	SER690
A	SER693
A	ACO805
A	HOH901
A	HOH902
A	HOH907
A	HOH961
A	HOH972

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	25
Details	Zinc finger: {"description":"C2HC MYST-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27768893","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"33657400","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21691301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27382063","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29321206","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PQ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DNC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J8F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WCI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29321206","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WCI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21691301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22547026","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22918831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27382063","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---