Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6C9M

The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue IHP A 901

Chain	Residue
A	LYS416
B	LYS78
A	LYS419
A	HIS420
A	LYS447
A	LYS450
A	TYR451
A	LYS454
B	HIS16
B	LYS51

site_id	AC2
Number of Residues	3
Details	binding site for residue 1PE C 901

Chain	Residue
C	GLU22
C	HIS80
C	GLN115

site_id	AC3
Number of Residues	10
Details	binding site for residue IHP C 902

Chain	Residue
C	LYS416
C	LYS419
C	HIS420
C	LYS447
C	LYS450
C	TYR451
C	LYS454
C	HOH1002
D	HIS16
D	LYS51

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	66
Details	Repeat: {"description":"TPR 1"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	66
Details	Repeat: {"description":"TPR 2"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	72
Details	Repeat: {"description":"TPR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	66
Details	Repeat: {"description":"TPR 4"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	66
Details	Repeat: {"description":"TPR 5"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	64
Details	Repeat: {"description":"TPR 6"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	66
Details	Repeat: {"description":"TPR 7"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	66
Details	Repeat: {"description":"TPR 8"}

Chain

Residue

Details

site_id	SWS_FT_FI9
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_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	302
Details	Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	114
Details	Region: {"description":"Interaction with NAA15","evidences":[{"source":"PubMed","id":"15496142","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
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)
		EDMap 2fo-fc (MTZ)