6WFO

Crystal structure of human Naa50 in complex with AcCoA and an inhibitor (compound 4b) identified using DNA encoded library technology

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	26
Details	binding site for residue ACO A 201

Chain	Residue
A	ILE26
A	ARG85
A	LEU86
A	GLY87
A	ILE88
A	GLY89
A	THR90
A	HIS112
A	ASN117
A	SER119
A	ALA120
A	PHE27
A	ASP122
A	PHE123
A	LYS126
A	U3Y202
A	HOH301
A	HOH305
A	HOH310
A	ILE74
A	MET75
A	THR76
A	LEU77
A	GLY78
A	CYS79
A	ARG84

---

site_id	AC2
Number of Residues	15
Details	binding site for residue U3Y A 202

Chain	Residue
A	PHE27
A	VAL29
A	TYR31
A	TYR73
A	MET75
A	HIS112
A	VAL113
A	GLN114
A	TYR138
A	TYR139
A	LYS140
A	ARG141
A	ACO201
A	HOH313
A	HOH320

---

site_id	AC3
Number of Residues	26
Details	binding site for residue ACO B 201

Chain	Residue
B	ILE26
B	PHE27
B	ILE74
B	MET75
B	THR76
B	LEU77
B	GLY78
B	CYS79
B	ARG84
B	ARG85
B	LEU86
B	GLY87
B	ILE88
B	GLY89
B	THR90
B	HIS112
B	ASN117
B	SER119
B	ASP122
B	PHE123
B	LYS126
B	U3Y202
B	HOH301
B	HOH303
B	HOH307
B	HOH332

---

site_id	AC4
Number of Residues	16
Details	binding site for residue U3Y B 202

Chain	Residue
B	PHE27
B	PRO28
B	VAL29
B	TYR31
B	ARG62
B	TYR73
B	MET75
B	HIS112
B	VAL113
B	GLN114
B	TYR138
B	TYR139
B	LYS140
B	ARG141
B	ACO201
B	HOH326

---

site_id	AC5
Number of Residues	27
Details	binding site for residue ACO C 201

Chain	Residue
C	SER119
C	ASP122
C	PHE123
C	LYS126
C	U3Y202
C	HOH301
C	HOH303
C	HOH305
C	HOH307
C	HOH311
C	HOH316
C	ILE26
C	PHE27
C	ILE74
C	THR76
C	LEU77
C	GLY78
C	CYS79
C	ARG84
C	ARG85
C	LEU86
C	GLY87
C	ILE88
C	GLY89
C	THR90
C	HIS112
C	ASN117

---

site_id	AC6
Number of Residues	17
Details	binding site for residue U3Y C 202

Chain	Residue
C	PHE27
C	VAL29
C	SER30
C	TYR31
C	ARG62
C	ASP64
C	TYR73
C	MET75
C	HIS112
C	VAL113
C	GLN114
C	TYR138
C	TYR139
C	LYS140
C	ARG141
C	ACO201
C	HOH308

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
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_FI3
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_FI4
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_FI5
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_FI6
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_FI7
Number of Residues	3
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---