5HGZ
Crystal structure of human Naa60 in complex with acetyl-CoA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000139 | cellular_component | Golgi membrane |
A | 0004402 | molecular_function | histone acetyltransferase activity |
A | 0004596 | molecular_function | peptide alpha-N-acetyltransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0006325 | biological_process | chromatin organization |
A | 0006334 | biological_process | nucleosome assembly |
A | 0006474 | biological_process | N-terminal protein amino acid acetylation |
A | 0007059 | biological_process | chromosome segregation |
A | 0008283 | biological_process | cell population proliferation |
A | 0010485 | molecular_function | histone H4 acetyltransferase activity |
A | 0016020 | cellular_component | membrane |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0017196 | biological_process | N-terminal peptidyl-methionine acetylation |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0061733 | molecular_function | peptide-lysine-N-acetyltransferase activity |
A | 0120518 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 30 |
Details | binding site for residue ACO A 301 |
Chain | Residue |
A | TRP33 |
A | GLY111 |
A | GLY113 |
A | SER114 |
A | HIS138 |
A | ASN143 |
A | THR145 |
A | ALA146 |
A | PHE149 |
A | TYR150 |
A | ASN152 |
A | PHE34 |
A | ARG153 |
A | TYR193 |
A | MLA302 |
A | HOH405 |
A | HOH413 |
A | HOH415 |
A | HOH424 |
A | HOH442 |
A | HOH457 |
A | HOH480 |
A | LEU99 |
A | HOH570 |
A | LEU101 |
A | GLY102 |
A | VAL103 |
A | ARG108 |
A | LYS109 |
A | HIS110 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue MLA A 302 |
Chain | Residue |
A | PHE34 |
A | TYR38 |
A | VAL139 |
A | LEU140 |
A | ASN143 |
A | TYR165 |
A | ACO301 |
A | HOH410 |
A | HOH516 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue MLA A 303 |
Chain | Residue |
A | ASP45 |
A | PHE52 |
A | LYS105 |
A | HOH401 |
A | HOH411 |
A | HOH441 |
A | HOH498 |
A | HOH513 |
A | HOH544 |
A | HOH571 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 196 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:25732826 |
Chain | Residue | Details |
A | MET1-ASP192 | |
A | GLU237-MET242 |
site_id | SWS_FT_FI2 |
Number of Residues | 43 |
Details | INTRAMEM: Helical => ECO:0000305|PubMed:25732826 |
Chain | Residue | Details |
A | TYR193-ILE236 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:27320834, ECO:0000269|PubMed:27550639 |
Chain | Residue | Details |
A | TYR97 | |
A | HIS138 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27320834, ECO:0000312|PDB:5ICV, ECO:0000312|PDB:5ICW |
Chain | Residue | Details |
A | TYR38 | |
A | LEU99 | |
A | TYR165 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | LEU101 | |
A | LYS109 | |
A | ASN143 | |
A | TYR150 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Required to position thioacetyl group => ECO:0000269|PubMed:27550639 |
Chain | Residue | Details |
A | PHE34 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21981917 |
Chain | Residue | Details |
A | LYS79 | |
A | LYS105 | |
A | LYS156 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000305|PubMed:21981917 |
Chain | Residue | Details |
A | LYS109 | |
A | LYS121 |