2Y0M

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE COMPENSATION FACTORS MSL1 AND MOF

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	0072487	cellular_component	MSL complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ACO A 1450

Chain	Residue
A	TRP192
A	ARG325
A	ARG326
A	GLY327
A	TYR328
A	GLY329
A	LYS330
A	SER354
A	LEU356
A	SER360
A	SER363
A	PHE270
A	TYR408
A	LYS432
A	HOH2009
A	HOH2010
A	LEU271
A	ALA315
A	CSO316
A	ILE317
A	LEU318
A	THR319
A	GLN324

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1451

Chain	Residue
A	CYS210
A	CYS213
A	HIS226
A	CYS230

---

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

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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

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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

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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

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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

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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

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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

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site_id	SWS_FT_FI9
Number of Residues	18
Details	Region: {"description":"Interaction with KAT8 HAT domain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01397","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	14
Details	Motif: {"description":"Bipartite nuclear localization signal","evidences":[{"source":"PubMed","id":"24913909","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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