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 | protein-N-terminal amino-acid acetyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 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 | 0017196 | biological_process | N-terminal peptidyl-methionine acetylation |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0061733 | molecular_function | protein-lysine-acetyltransferase activity |
| A | 0120518 | molecular_function | protein N-terminal-methionine acetyltransferase activity |
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 | 191 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25732826","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 169 |
| Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Region: {"description":"Required for homodimerization","evidences":[{"source":"PubMed","id":"27320834","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"27320834","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27550639","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27320834","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ICV","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5ICW","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27320834","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27550639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5HGZ","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5HH0","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5HH1","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5ICV","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5ICW","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Required to position thioacetyl group","evidences":[{"source":"PubMed","id":"27550639","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"21981917","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"21981917","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
