5J9W

Crystal structure of the NuA4 core complex

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	0000123	cellular_component	histone acetyltransferase complex
B	0004402	molecular_function	histone acetyltransferase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0006281	biological_process	DNA repair
B	0006325	biological_process	chromatin organization
B	0006338	biological_process	chromatin remodeling
B	0006351	biological_process	DNA-templated transcription
B	0006974	biological_process	DNA damage response
B	0033100	cellular_component	NuA3 histone acetyltransferase complex
B	0035267	cellular_component	NuA4 histone acetyltransferase complex
B	1990467	cellular_component	NuA3a histone acetyltransferase complex
B	1990468	cellular_component	NuA3b histone acetyltransferase complex
C	0006357	biological_process	regulation of transcription by RNA polymerase II
C	0035267	cellular_component	NuA4 histone acetyltransferase complex
E	0004402	molecular_function	histone acetyltransferase activity
E	0006355	biological_process	regulation of DNA-templated transcription
F	0000123	cellular_component	histone acetyltransferase complex
F	0004402	molecular_function	histone acetyltransferase activity
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0006281	biological_process	DNA repair
F	0006325	biological_process	chromatin organization
F	0006338	biological_process	chromatin remodeling
F	0006351	biological_process	DNA-templated transcription
F	0006974	biological_process	DNA damage response
F	0033100	cellular_component	NuA3 histone acetyltransferase complex
F	0035267	cellular_component	NuA4 histone acetyltransferase complex
F	1990467	cellular_component	NuA3a histone acetyltransferase complex
F	1990468	cellular_component	NuA3b histone acetyltransferase complex
G	0006357	biological_process	regulation of transcription by RNA polymerase II
G	0035267	cellular_component	NuA4 histone acetyltransferase complex
I	0004402	molecular_function	histone acetyltransferase activity
I	0006355	biological_process	regulation of DNA-templated transcription
J	0000123	cellular_component	histone acetyltransferase complex
J	0004402	molecular_function	histone acetyltransferase activity
J	0005515	molecular_function	protein binding
J	0005634	cellular_component	nucleus
J	0006281	biological_process	DNA repair
J	0006325	biological_process	chromatin organization
J	0006338	biological_process	chromatin remodeling
J	0006351	biological_process	DNA-templated transcription
J	0006974	biological_process	DNA damage response
J	0033100	cellular_component	NuA3 histone acetyltransferase complex
J	0035267	cellular_component	NuA4 histone acetyltransferase complex
J	1990467	cellular_component	NuA3a histone acetyltransferase complex
J	1990468	cellular_component	NuA3b histone acetyltransferase complex
K	0006357	biological_process	regulation of transcription by RNA polymerase II
K	0035267	cellular_component	NuA4 histone acetyltransferase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue ACO E 500

Chain	Residue
E	PHE258
E	GLY317
E	LYS318
E	PRO340
E	LEU341
E	SER342
E	LEU344
E	GLY345
E	LEU347
E	SER348
E	ARG421
E	LEU259
E	ALA303
E	ILE305
E	LEU306
E	THR307
E	GLN312
E	ARG313
E	GLY315

---

site_id	AC2
Number of Residues	21
Details	binding site for residue ACO I 500

Chain	Residue
I	TRP180
I	PHE258
I	LEU259
I	ILE305
I	LEU306
I	THR307
I	GLN312
I	ARG313
I	MET314
I	GLY315
I	TYR316
I	GLY317
I	LYS318
I	GLN338
I	SER342
I	LEU344
I	GLY345
I	LEU347
I	SER348
I	ALA351
I	ARG421

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	75
Details	Zinc finger: {"description":"C2HC MYST-type; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"17223684","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"18245364","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000303"},{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	33
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11106757","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	195
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 525

Chain	Residue	Details
A	LEU308	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	SER342	activator, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	2
Details	M-CSA 525

Chain	Residue	Details
E	LEU308	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
E	SER342	activator, proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	2
Details	M-CSA 525

Chain	Residue	Details
I	LEU308	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
I	SER342	activator, proton acceptor, proton donor

---