3TFY

Naa50p amino-terminal acetyltransferase bound to substrate peptide fragment and CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004596	molecular_function	protein-N-terminal amino-acid acetyltransferase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006338	biological_process	chromatin remodeling
A	0006474	biological_process	N-terminal protein amino acid acetylation
A	0007064	biological_process	mitotic sister chromatid cohesion
A	0010485	molecular_function	histone H4 acetyltransferase activity
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0031415	cellular_component	NatA complex
A	0034087	biological_process	establishment of mitotic sister chromatid cohesion
A	0043687	biological_process	post-translational protein modification
A	0061733	molecular_function	protein-lysine-acetyltransferase activity
A	0070062	cellular_component	extracellular exosome
A	0071962	biological_process	mitotic sister chromatid cohesion, centromeric
A	0120518	molecular_function	protein N-terminal-methionine acetyltransferase activity
B	0004596	molecular_function	protein-N-terminal amino-acid acetyltransferase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005730	cellular_component	nucleolus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006338	biological_process	chromatin remodeling
B	0006474	biological_process	N-terminal protein amino acid acetylation
B	0007064	biological_process	mitotic sister chromatid cohesion
B	0010485	molecular_function	histone H4 acetyltransferase activity
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0031415	cellular_component	NatA complex
B	0034087	biological_process	establishment of mitotic sister chromatid cohesion
B	0043687	biological_process	post-translational protein modification
B	0061733	molecular_function	protein-lysine-acetyltransferase activity
B	0070062	cellular_component	extracellular exosome
B	0071962	biological_process	mitotic sister chromatid cohesion, centromeric
B	0120518	molecular_function	protein N-terminal-methionine acetyltransferase activity
C	0004596	molecular_function	protein-N-terminal amino-acid acetyltransferase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006338	biological_process	chromatin remodeling
C	0006474	biological_process	N-terminal protein amino acid acetylation
C	0007064	biological_process	mitotic sister chromatid cohesion
C	0010485	molecular_function	histone H4 acetyltransferase activity
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0031415	cellular_component	NatA complex
C	0034087	biological_process	establishment of mitotic sister chromatid cohesion
C	0043687	biological_process	post-translational protein modification
C	0061733	molecular_function	protein-lysine-acetyltransferase activity
C	0070062	cellular_component	extracellular exosome
C	0071962	biological_process	mitotic sister chromatid cohesion, centromeric
C	0120518	molecular_function	protein N-terminal-methionine acetyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE COA A 201

Chain	Residue
A	PHE27
A	GLY89
A	THR90
A	ASN117
A	SER119
A	ASP122
A	PHE123
A	TYR124
A	LYS126
A	HOH170
A	HOH171
A	LEU77
A	HOH177
A	HOH180
A	HOH188
D	MET5122
A	GLY78
A	CYS79
A	ARG84
A	ARG85
A	LEU86
A	GLY87
A	ILE88

---

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE COA B 201

Chain	Residue
B	ILE26
B	LEU77
B	GLY78
B	CYS79
B	ARG84
B	ARG85
B	LEU86
B	GLY87
B	ILE88
B	GLY89
B	THR90
B	ASN117
B	SER119
B	ASP122
B	PHE123
B	LYS126
B	HOH171
B	HOH172
B	HOH176
B	HOH183
B	HOH187
E	MET5122

---

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE COA C 201

Chain	Residue
C	PHE27
C	LEU77
C	GLY78
C	CYS79
C	ARG84
C	ARG85
C	LEU86
C	GLY87
C	ILE88
C	GLY89
C	THR90
C	LEU111
C	ASN117
C	SER119
C	PHE123
C	TYR124
C	LYS126
C	HOH177
C	HOH178
F	MET5122

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	447
Details	Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27484799","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X5K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	66
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27484799","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2007","submissionDatabase":"PDB data bank","title":"Structure of human MAK3 homolog.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2PSW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X5K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	Modified residue: {"description":"N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Zebisch A.","Kolch W."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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