Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PPL

Cryo-EM structure of human NatE complex (NatA/Naa50)

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	0001525	biological_process	angiogenesis
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005667	cellular_component	transcription regulator complex
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006351	biological_process	DNA-templated transcription
B	0010698	molecular_function	acetyltransferase activator activity
B	0016020	cellular_component	membrane
B	0016407	molecular_function	acetyltransferase activity
B	0016604	cellular_component	nuclear body
B	0030154	biological_process	cell differentiation
B	0031415	cellular_component	NatA complex
B	0043022	molecular_function	ribosome binding
B	0045893	biological_process	positive regulation of DNA-templated transcription
B	0050821	biological_process	protein stabilization
B	0051604	biological_process	protein maturation
C	0004596	molecular_function	protein-N-terminal amino-acid acetyltransferase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006474	biological_process	N-terminal protein amino acid acetylation
C	0008080	molecular_function	N-acetyltransferase activity
C	0008999	molecular_function	protein-N-terminal-alanine acetyltransferase activity
C	0016020	cellular_component	membrane
C	0016407	molecular_function	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	0043022	molecular_function	ribosome binding
C	0051604	biological_process	protein maturation
C	1904592	biological_process	positive regulation of protein refolding
C	1990189	molecular_function	protein N-terminal-serine acetyltransferase activity
C	1990190	molecular_function	protein-N-terminal-glutamate acetyltransferase activity
C	2000719	biological_process	negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue ACO A 201

Chain	Residue
A	ILE26
A	GLY89
A	THR90
A	HIS112
A	VAL113
A	GLN114
A	ASN117
A	SER119
A	PHE123
A	LYS126
A	LEU77
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 IHP B 901

Chain	Residue
B	LYS416
B	LYS419
B	HIS420
B	LYS447
B	LYS450
B	TYR451
B	LYS556
C	HIS16
C	LYS51
C	LYS78
C	SER80

site_id	AC3
Number of Residues	16
Details	binding site for residue ACO C 901

Chain	Residue
A	ASP53
C	LEU22
C	LEU75
C	ALA76
C	VAL77
C	ARG82
C	ARG83
C	GLY85
C	LEU86
C	ALA87
C	GLN88
C	ALA117
C	HIS120
C	LEU121
C	TYR122
C	THR125

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	300
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	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"21900231","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
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	22
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	1
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	4
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	1
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	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
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	36
Details	Repeat: {"description":"TPR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	33
Details	Repeat: {"description":"TPR 4"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	33
Details	Repeat: {"description":"TPR 5"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	32
Details	Repeat: {"description":"TPR 6"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	33
Details	Repeat: {"description":"TPR 7"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	33
Details	Repeat: {"description":"TPR 8"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	57
Details	Region: {"description":"Interaction with NAA15","evidences":[{"source":"PubMed","id":"15496142","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"27708256","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)