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6HD5

Cryo-EM structure of the ribosome-NatA complex

Functional Information from GO Data
ChainGOidnamespacecontents
t0004596molecular_functionpeptide alpha-N-acetyltransferase activity
t0005515molecular_functionprotein binding
t0005737cellular_componentcytoplasm
t0005739cellular_componentmitochondrion
t0006474biological_processN-terminal protein amino acid acetylation
t0031415cellular_componentNatA complex
t0043022molecular_functionribosome binding
u0004596molecular_functionpeptide alpha-N-acetyltransferase activity
u0005515molecular_functionprotein binding
u0005737cellular_componentcytoplasm
u0006474biological_processN-terminal protein amino acid acetylation
u0016740molecular_functiontransferase activity
u0016746molecular_functionacyltransferase activity
u0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
u0031415cellular_componentNatA complex
u0042802molecular_functionidentical protein binding
u0061606biological_processN-terminal protein amino acid propionylation
u1990189molecular_functionpeptide-serine-alpha-N-acetyltransferase activity
u1990190molecular_functionpeptide-glutamate-alpha-N-acetyltransferase activity
v0004596molecular_functionpeptide alpha-N-acetyltransferase activity
v0005737cellular_componentcytoplasm
v0006474biological_processN-terminal protein amino acid acetylation
v0007064biological_processmitotic sister chromatid cohesion
v0008080molecular_functionN-acetyltransferase activity
v0016740molecular_functiontransferase activity
v0016746molecular_functionacyltransferase activity
v0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
v0031415cellular_componentNatA complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000255
ChainResidueDetails
tSER2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
tSER674

218853

PDB entries from 2024-04-24

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