6WF3

Crystal structure of human Naa50 in complex with a cofactor derived inhibitor (compound 1)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for Di-peptide ACE G 1 and MET G 2

Chain	Residue
A	PHE27
A	TYR139
A	HOH210
G	LEU3
G	GLY4
G	COA101
A	PRO28
A	VAL29
A	TYR31
A	ILE74
A	MET75
A	THR76
A	LEU77
A	HIS112

---

site_id	AC2
Number of Residues	3
Details	binding site for Di-peptide PRO G 5 and NH2 G 6

Chain	Residue
A	SER30
G	LEU3
G	GLY4

---

site_id	AC3
Number of Residues	27
Details	binding site for residues COA G 101 and ACE G 1

Chain	Residue
A	ILE26
A	PHE27
A	ILE74
A	MET75
A	THR76
A	LEU77
A	GLY78
A	CYS79
A	ARG84
A	ARG85
A	LEU86
A	GLY87
A	ILE88
A	GLY89
A	THR90
A	VAL113
A	ASN117
A	SER119
A	ASP122
A	PHE123
A	TYR124
A	LYS126
A	HOH201
G	MET2
G	HOH201
G	HOH202
G	HOH203

---

site_id	AC4
Number of Residues	14
Details	binding site for Di-peptide ACE O 1 and MET O 2

Chain	Residue
B	PHE27
B	PRO28
B	VAL29
B	TYR31
B	MET75
B	THR76
B	LEU77
B	HIS112
B	GLN114
B	TYR139
B	HOH205
H	LEU3
H	GLY4
H	COA101

---

site_id	AC5
Number of Residues	3
Details	binding site for Di-peptide PRO O 5 and NH2 O 6

Chain	Residue
B	SER30
H	LEU3
H	GLY4

---

site_id	AC6
Number of Residues	28
Details	binding site for residues COA O 101 and ACE O 1

Chain	Residue
B	ILE26
B	PHE27
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	VAL113
B	ASN117
B	SER119
B	ALA120
B	ASP122
B	PHE123
B	TYR124
B	LYS126
B	HOH201
H	MET2
H	HOH201
H	HOH202
H	HOH203
H	HOH204

---

site_id	AC7
Number of Residues	13
Details	binding site for Di-peptide ACE P 1 and MET P 2

Chain	Residue
I	LEU3
I	GLY4
I	COA101
C	PHE27
C	PRO28
C	TYR31
C	ILE74
C	MET75
C	THR76
C	LEU77
C	HIS112
C	TYR139
C	HOH216

---

site_id	AC8
Number of Residues	3
Details	binding site for Di-peptide PRO P 5 and NH2 P 6

Chain	Residue
C	SER30
I	LEU3
I	GLY4

---

site_id	AC9
Number of Residues	29
Details	binding site for residues COA P 101 and ACE P 1

Chain	Residue
C	ILE26
C	PHE27
C	ILE74
C	MET75
C	THR76
C	LEU77
C	GLY78
C	CYS79
C	ARG84
C	ARG85
C	LEU86
C	GLY87
C	GLY89
C	THR90
C	ASN117
C	SER119
C	ALA120
C	ASP122
C	PHE123
C	TYR124
C	LYS126
C	HOH202
I	MET2
I	HOH201
I	HOH202
I	HOH203
I	HOH204
I	HOH205
I	HOH206

---

site_id	AD1
Number of Residues	14
Details	binding site for Di-peptide ACE Q 1 and MET Q 2

Chain	Residue
D	PHE27
D	PRO28
D	VAL29
D	TYR31
D	MET75
D	THR76
D	LEU77
D	HIS112
D	GLN114
D	TYR139
D	HOH218
J	LEU3
J	GLY4
J	COA101

---

site_id	AD2
Number of Residues	5
Details	binding site for Di-peptide PRO Q 5 and NH2 Q 6

Chain	Residue
D	HOH250
J	LEU3
J	GLY4
J	HOH205
J	HOH206

---

site_id	AD3
Number of Residues	28
Details	binding site for residues COA Q 101 and ACE Q 1

Chain	Residue
D	ILE26
D	PHE27
D	MET75
D	THR76
D	LEU77
D	GLY78
D	CYS79
D	ARG84
D	ARG85
D	LEU86
D	GLY87
D	ILE88
D	GLY89
D	THR90
D	HIS112
D	ASN117
D	SER119
D	ASP122
D	PHE123
D	TYR124
D	LYS126
D	HOH203
J	MET2
J	HOH201
J	HOH202
J	HOH203
J	HOH204
J	HOH207

---

site_id	AD4
Number of Residues	12
Details	binding site for Di-peptide ACE R 1 and MET R 2

Chain	Residue
E	PHE27
E	PRO28
E	TYR31
E	ILE74
E	MET75
E	THR76
E	LEU77
E	HIS112
E	TYR139
K	LEU3
K	GLY4
K	COA101

---

site_id	AD5
Number of Residues	3
Details	binding site for Di-peptide PRO R 5 and NH2 R 6

Chain	Residue
E	SER30
K	LEU3
K	GLY4

---

site_id	AD6
Number of Residues	28
Details	binding site for residues COA R 101 and ACE R 1

Chain	Residue
E	ILE26
E	PHE27
E	ILE74
E	MET75
E	THR76
E	LEU77
E	GLY78
E	CYS79
E	ARG84
E	ARG85
E	LEU86
E	GLY87
E	ILE88
E	GLY89
E	THR90
E	HIS112
E	VAL113
E	ASN117
E	SER119
E	ALA120
E	ASP122
E	PHE123
E	TYR124
E	LYS126
K	MET2
K	HOH201
K	HOH202
K	HOH203

---

site_id	AD7
Number of Residues	11
Details	binding site for Di-peptide ACE S 1 and MET S 2

Chain	Residue
F	PHE27
F	PRO28
F	TYR31
F	MET75
F	THR76
F	LEU77
F	HIS112
F	TYR139
F	HOH204
L	LEU3
L	COA101

---

site_id	AD8
Number of Residues	3
Details	binding site for Di-peptide PRO S 5 and NH2 S 6

Chain	Residue
F	SER30
L	LEU3
L	GLY4

---

site_id	AD9
Number of Residues	26
Details	binding site for residues COA S 101 and ACE S 1

Chain	Residue
F	ILE26
F	PHE27
F	MET75
F	THR76
F	LEU77
F	GLY78
F	CYS79
F	ARG84
F	ARG85
F	LEU86
F	GLY87
F	ILE88
F	GLY89
F	THR90
F	ASN117
F	SER119
F	ALA120
F	ASP122
F	PHE123
F	TYR124
F	LYS126
F	HOH201
L	MET2
L	HOH201
L	HOH202
L	HOH203

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	30
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	132
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	6
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	6
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	6
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	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"19744929","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---