Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019843 | molecular_function | rRNA binding |
| A | 0042254 | biological_process | ribosome biogenesis |
| A | 0042274 | biological_process | ribosomal small subunit biogenesis |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue G4P A 301 |
| Chain | Residue |
| A | ARG28 |
| A | SER166 |
| A | GLY167 |
| A | VAL168 |
| A | GLY169 |
| A | LYS170 |
| A | SER171 |
| A | THR172 |
| A | HOH465 |
| A | HOH466 |
| A | ARG32 |
| A | LYS113 |
| A | ASP115 |
| A | LYS116 |
| A | GLY143 |
| A | ASN144 |
| A | ARG148 |
| A | GLN165 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | CYS245 |
| A | CYS250 |
| A | HIS252 |
| A | CYS258 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ARG68 |
| A | TYR103 |
| A | PHE218 |
| A | ALA220 |
| A | ASP222 |
| A | HOH451 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | SER89 |
| A | THR90 |
| A | GLN91 |
| A | EDO305 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | HIS276 |
| A | EDO304 |
| A | HOH447 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | ASN134 |
| A | GLY267 |
| A | ALA270 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 307 |
| Chain | Residue |
| A | ARG108 |
| A | GLU138 |
| A | ALA154 |
| A | TRP155 |
| A | PRO156 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 308 |
| Chain | Residue |
| A | ASN134 |
| A | ILE135 |
| A | GLU237 |
| A | ARG240 |
| A | ASN268 |
| A | HOH409 |
| A | HOH429 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 309 |
| Chain | Residue |
| A | GLU133 |
| A | THR139 |
| A | GLU140 |
| A | HOH416 |
| A | HOH422 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue PGE A 310 |
| Chain | Residue |
| A | LYS35 |
| A | PHE36 |
| A | VAL59 |
Functional Information from PROSITE/UniProt
| site_id | PS00675 |
| Number of Residues | 14 |
| Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. IVLsGQSGVGKstF |
| Chain | Residue | Details |
| A | ILE160-PHE173 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01820","evidenceCode":"ECO:0000255"}]} |
