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5HGZ

Crystal structure of human Naa60 in complex with acetyl-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0004402molecular_functionhistone acetyltransferase activity
A0004596molecular_functionpeptide alpha-N-acetyltransferase activity
A0005515molecular_functionprotein binding
A0005794cellular_componentGolgi apparatus
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0006474biological_processN-terminal protein amino acid acetylation
A0007059biological_processchromosome segregation
A0008283biological_processcell population proliferation
A0010485molecular_functionhistone H4 acetyltransferase activity
A0016020cellular_componentmembrane
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0017196biological_processN-terminal peptidyl-methionine acetylation
A0042803molecular_functionprotein homodimerization activity
A0061733molecular_functionpeptide-lysine-N-acetyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues30
Detailsbinding site for residue ACO A 301
ChainResidue
ATRP33
AGLY111
AGLY113
ASER114
AHIS138
AASN143
ATHR145
AALA146
APHE149
ATYR150
AASN152
APHE34
AARG153
ATYR193
AMLA302
AHOH405
AHOH413
AHOH415
AHOH424
AHOH442
AHOH457
AHOH480
ALEU99
AHOH570
ALEU101
AGLY102
AVAL103
AARG108
ALYS109
AHIS110

site_idAC2
Number of Residues9
Detailsbinding site for residue MLA A 302
ChainResidue
APHE34
ATYR38
AVAL139
ALEU140
AASN143
ATYR165
AACO301
AHOH410
AHOH516

site_idAC3
Number of Residues10
Detailsbinding site for residue MLA A 303
ChainResidue
AASP45
APHE52
ALYS105
AHOH401
AHOH411
AHOH441
AHOH498
AHOH513
AHOH544
AHOH571

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues196
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:25732826
ChainResidueDetails
AMET1-ASP192
AGLU237-MET242

site_idSWS_FT_FI2
Number of Residues43
DetailsINTRAMEM: Helical => ECO:0000305|PubMed:25732826
ChainResidueDetails
ATYR193-ILE236

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:27320834, ECO:0000269|PubMed:27550639
ChainResidueDetails
ATYR97
AHIS138

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27320834, ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW
ChainResidueDetails
ATYR165
ATYR38
ALEU99

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27320834, ECO:0000269|PubMed:27550639, ECO:0000312|PDB:5HGZ, ECO:0000312|PDB:5HH0, ECO:0000312|PDB:5HH1, ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW
ChainResidueDetails
ALYS109
AASN143
ATYR150
ALEU101

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Required to position thioacetyl group => ECO:0000269|PubMed:27550639
ChainResidueDetails
APHE34

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21981917
ChainResidueDetails
ALYS105
ALYS156
ALYS79

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000305|PubMed:21981917
ChainResidueDetails
ALYS109
ALYS121

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PDB entries from 2024-05-15

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