6WFG

Crystal structure of human Naa50 in complex with an inhibitor (compound 3) identified using DNA encoded library technology

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004596	molecular_function	peptide alpha-N-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	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	0052858	molecular_function	peptidyl-lysine acetyltransferase activity
A	0070062	cellular_component	extracellular exosome
A	0071962	biological_process	mitotic sister chromatid cohesion, centromeric
C	0004596	molecular_function	peptide alpha-N-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	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	0052858	molecular_function	peptidyl-lysine acetyltransferase activity
C	0070062	cellular_component	extracellular exosome
C	0071962	biological_process	mitotic sister chromatid cohesion, centromeric
E	0004596	molecular_function	peptide alpha-N-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	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	0052858	molecular_function	peptidyl-lysine acetyltransferase activity
E	0070062	cellular_component	extracellular exosome
E	0071962	biological_process	mitotic sister chromatid cohesion, centromeric

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
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	LYS126
A	HOH301
A	HOH302
A	HOH304
A	LEU77
A	HOH313
A	GLY78
A	CYS79
A	ARG84
A	ARG85
A	LEU86
A	GLY87
A	ILE88

---

site_id	AC2
Number of Residues	11
Details	binding site for residue U3V A 202

Chain	Residue
A	VAL29
A	TYR31
A	ARG62
A	ASP64
A	TYR73
A	MET75
A	TYR110
A	HIS112
A	GLN114
A	TYR138
A	TYR139

---

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	ASN117
C	SER119
C	ASP122
C	PHE123
C	LYS126
C	HOH301
C	HOH303
C	HOH306
C	HOH308

---

site_id	AC4
Number of Residues	12
Details	binding site for residue U3V C 202

Chain	Residue
C	TYR31
C	ARG62
C	ASP64
C	TYR73
C	MET75
C	TYR110
C	HIS112
C	VAL113
C	GLN114
C	TYR138
C	TYR139
C	HOH310

---

site_id	AC5
Number of Residues	19
Details	binding site for residue COA E 201

Chain	Residue
E	PHE27
E	LEU77
E	GLY78
E	CYS79
E	ARG84
E	ARG85
E	LEU86
E	GLY87
E	GLY89
E	THR90
E	ASN117
E	SER119
E	ASP122
E	PHE123
E	TYR124
E	LYS126
E	HOH301
E	HOH302
E	HOH305

---

site_id	AC6
Number of Residues	13
Details	binding site for residue U3V E 202

Chain	Residue
E	VAL29
E	TYR31
E	ARG62
E	ASP64
E	TYR73
E	MET75
E	TYR110
E	HIS112
E	VAL113
E	GLN114
E	TYR138
E	TYR139
E	HOH311

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:21900231

Chain	Residue	Details
A	TYR73
A	HIS112
C	TYR73
C	HIS112
E	TYR73
E	HIS112

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:27484799, ECO:0007744|PDB:3TFY, ECO:0007744|PDB:4X5K

Chain	Residue	Details
A	TYR31
A	MET75
A	TYR138
C	TYR31
C	MET75
C	TYR138
E	TYR31
E	MET75
E	TYR138

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:27484799, ECO:0000269|Ref.19, ECO:0007744|PDB:2PSW, ECO:0007744|PDB:3TFY, ECO:0007744|PDB:4X5K

Chain	Residue	Details
A	LEU77
A	ASN117
C	LEU77
C	ASN117
E	LEU77
E	ASN117

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR12
C	THR12
E	THR12

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:19744929, ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS34
A	LYS37
C	LYS34
C	LYS37
E	LYS34
E	LYS37

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR110
C	TYR110
E	TYR110

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:19744929

Chain	Residue	Details
A	LYS140
C	LYS140
E	LYS140

---