6CY6
Crystal structure of spermidine/spermine N-acetyltransferase SpeG from Escherichia coli in complex with tris(hydroxymethyl)aminomethane.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004145 | molecular_function | diamine N-acetyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006598 | biological_process | polyamine catabolic process |
| A | 0015936 | biological_process | coenzyme A metabolic process |
| 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 | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046203 | biological_process | spermidine catabolic process |
| A | 0046208 | biological_process | spermine catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 201 |
| Chain | Residue |
| A | GLU15 |
| A | ARG18 |
| A | HOH332 |
| A | HOH404 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 202 |
| Chain | Residue |
| A | MET30 |
| A | ARG31 |
| A | TYR32 |
| A | ARG59 |
| A | HOH333 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 203 |
| Chain | Residue |
| A | ASP125 |
| A | ASN128 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 204 |
| Chain | Residue |
| A | ARG31 |
| A | MPD212 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 205 |
| Chain | Residue |
| A | ARG14 |
| A | SER45 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 206 |
| Chain | Residue |
| A | LYS126 |
| A | ARG136 |
| A | VAL142 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 207 |
| Chain | Residue |
| A | TYR156 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 208 |
| Chain | Residue |
| A | ARG14 |
| A | HOH404 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 209 |
| Chain | Residue |
| A | GLU36 |
| A | ASP54 |
| A | GLU57 |
| A | ARG58 |
| A | HOH321 |
| A | HOH365 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue TRS A 210 |
| Chain | Residue |
| A | TYR32 |
| A | TRP33 |
| A | ASP54 |
| A | SER56 |
| A | GLU57 |
| A | GLU76 |
| A | HOH302 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MRD A 211 |
| Chain | Residue |
| A | LEU12 |
| A | HIS51 |
| A | GLU57 |
| A | ARG58 |
| A | ARG59 |
| A | HOH321 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue MPD A 212 |
| Chain | Residue |
| A | CL204 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue MRD A 213 |
| Chain | Residue |
| A | ASN128 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue MPD A 214 |
| Chain | Residue |
| A | TYR32 |
| A | ILE123 |
| A | LEU146 |
| A | GLU149 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue MPD A 215 |
| Chain | Residue |
| A | LYS126 |
| A | GLU143 |
| A | GLU145 |
| A | ILE160 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue MPD A 216 |
| Chain | Residue |
| A | ILE123 |
| A | ASP125 |
| A | PHE150 |
| A | ILE152 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"33826189","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 25 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9KL03","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31205017","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R9M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Could be important for selectivity toward long polyamines","evidences":[{"source":"UniProtKB","id":"Q9KL03","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
