4J6W
Crystal structure of HFQ from Pseudomonas aeruginosa in complex with CTP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006417 | biological_process | regulation of translation |
| A | 0009372 | biological_process | quorum sensing |
| A | 0043487 | biological_process | regulation of RNA stability |
| A | 0043609 | biological_process | regulation of carbon utilization |
| A | 0045974 | biological_process | regulation of translation, ncRNA-mediated |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006417 | biological_process | regulation of translation |
| B | 0009372 | biological_process | quorum sensing |
| B | 0043487 | biological_process | regulation of RNA stability |
| B | 0043609 | biological_process | regulation of carbon utilization |
| B | 0045974 | biological_process | regulation of translation, ncRNA-mediated |
| C | 0003723 | molecular_function | RNA binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0006417 | biological_process | regulation of translation |
| C | 0009372 | biological_process | quorum sensing |
| C | 0043487 | biological_process | regulation of RNA stability |
| C | 0043609 | biological_process | regulation of carbon utilization |
| C | 0045974 | biological_process | regulation of translation, ncRNA-mediated |
| D | 0003723 | molecular_function | RNA binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0006417 | biological_process | regulation of translation |
| D | 0009372 | biological_process | quorum sensing |
| D | 0043487 | biological_process | regulation of RNA stability |
| D | 0043609 | biological_process | regulation of carbon utilization |
| D | 0045974 | biological_process | regulation of translation, ncRNA-mediated |
| E | 0003723 | molecular_function | RNA binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0006417 | biological_process | regulation of translation |
| E | 0009372 | biological_process | quorum sensing |
| E | 0043487 | biological_process | regulation of RNA stability |
| E | 0043609 | biological_process | regulation of carbon utilization |
| E | 0045974 | biological_process | regulation of translation, ncRNA-mediated |
| F | 0003723 | molecular_function | RNA binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0006417 | biological_process | regulation of translation |
| F | 0009372 | biological_process | quorum sensing |
| F | 0043487 | biological_process | regulation of RNA stability |
| F | 0043609 | biological_process | regulation of carbon utilization |
| F | 0045974 | biological_process | regulation of translation, ncRNA-mediated |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CTP A 101 |
| Chain | Residue |
| A | TYR25 |
| C | ARG69 |
| E | ASN28 |
| E | ILE30 |
| A | GLY29 |
| A | LYS31 |
| A | THR61 |
| A | HOH203 |
| A | HOH221 |
| A | HOH234 |
| A | HOH244 |
| A | HOH245 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE C5P A 102 |
| Chain | Residue |
| A | HIS5 |
| A | GLN8 |
| A | GLN41 |
| A | PHE42 |
| A | LYS56 |
| A | HOH233 |
| A | HOH240 |
| A | HOH250 |
| A | HOH260 |
| B | CTP101 |
| B | HOH236 |
| E | PHE42 |
| E | HIS57 |
| E | C5P101 |
| E | MG104 |
| E | MG105 |
| E | HOH229 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 103 |
| Chain | Residue |
| A | ASP9 |
| A | PHE39 |
| A | ASP40 |
| A | LYS56 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 104 |
| Chain | Residue |
| D | P6G103 |
| D | HOH227 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE CTP B 101 |
| Chain | Residue |
| A | PHE42 |
| A | TYR55 |
| A | HIS57 |
| A | C5P102 |
| A | HOH240 |
| A | HOH260 |
| B | HIS5 |
| B | GLN8 |
| B | GLN41 |
| B | PHE42 |
| B | LYS56 |
| B | HIS57 |
| B | MG102 |
| B | HOH206 |
| B | HOH220 |
| B | HOH221 |
| B | HOH222 |
| B | HOH236 |
| B | HOH237 |
| B | HOH238 |
| C | MG103 |
| C | MG104 |
| D | C5P101 |
| D | MG105 |
| D | HOH208 |
| E | C5P101 |
| E | MG105 |
| E | HOH229 |
| F | CDP101 |
| F | HOH228 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 102 |
| Chain | Residue |
| B | CTP101 |
| B | HOH222 |
| B | HOH236 |
| D | C5P101 |
| D | HOH226 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CTP C 101 |
| Chain | Residue |
| C | TYR25 |
| C | GLY29 |
| C | LYS31 |
| C | SER60 |
| C | THR61 |
| C | HOH202 |
| C | HOH230 |
| C | HOH236 |
| C | HOH243 |
| F | ASN28 |
| F | ILE30 |
| F | HOH202 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE C5P C 102 |
| Chain | Residue |
| C | HIS5 |
| C | GLN8 |
| C | GLN41 |
| C | PHE42 |
| C | LYS56 |
| C | MG103 |
| C | MG104 |
| C | HOH224 |
| E | C5P101 |
| F | PHE42 |
| F | TYR55 |
| F | HIS57 |
| F | CDP101 |
| F | NA105 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 103 |
| Chain | Residue |
| E | C5P101 |
| F | CDP101 |
| B | CTP101 |
| C | C5P102 |
| C | MG104 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG C 104 |
| Chain | Residue |
| A | HOH260 |
| B | CTP101 |
| B | HOH237 |
| C | C5P102 |
| C | MG103 |
| D | C5P101 |
| F | CDP101 |
| F | NA105 |
| site_id | BC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE C5P D 101 |
| Chain | Residue |
| B | PHE42 |
| B | HIS57 |
| B | CTP101 |
| B | MG102 |
| B | HOH237 |
| C | MG104 |
| D | HIS5 |
| D | GLN8 |
| D | GLN41 |
| D | PHE42 |
| D | LYS56 |
| D | HIS57 |
| D | MG104 |
| D | MG105 |
| D | HOH226 |
| F | CDP101 |
| F | NA105 |
| site_id | BC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CTP D 102 |
| Chain | Residue |
| B | LEU26 |
| B | ASN28 |
| B | ILE30 |
| B | HOH203 |
| C | GLN35 |
| C | ASN48 |
| D | TYR25 |
| D | GLY29 |
| D | LYS31 |
| D | SER60 |
| D | THR61 |
| D | HOH202 |
| D | HOH219 |
| D | HOH221 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE P6G D 103 |
| Chain | Residue |
| A | NA104 |
| B | VAL27 |
| C | ARG66 |
| D | VAL27 |
| D | HOH227 |
| F | VAL27 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 104 |
| Chain | Residue |
| D | PHE42 |
| D | LYS56 |
| D | HIS57 |
| D | C5P101 |
| F | CDP101 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 105 |
| Chain | Residue |
| B | CTP101 |
| B | HOH220 |
| D | C5P101 |
| F | CDP101 |
| site_id | BC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE C5P E 101 |
| Chain | Residue |
| A | C5P102 |
| A | HOH233 |
| A | HOH260 |
| B | CTP101 |
| C | PHE42 |
| C | TYR55 |
| C | HIS57 |
| C | C5P102 |
| C | MG103 |
| C | HOH207 |
| E | GLY4 |
| E | GLN8 |
| E | GLN41 |
| E | PHE42 |
| E | LYS56 |
| E | HIS57 |
| E | MG104 |
| E | MG105 |
| E | HOH204 |
| E | HOH229 |
| site_id | BC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CTP E 102 |
| Chain | Residue |
| C | ASN28 |
| C | ILE30 |
| C | HOH204 |
| E | TYR25 |
| E | GLY29 |
| E | LYS31 |
| E | SER60 |
| E | THR61 |
| E | HOH201 |
| E | HOH209 |
| E | HOH217 |
| E | HOH227 |
| E | HOH230 |
| E | HOH237 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL E 103 |
| Chain | Residue |
| E | LYS31 |
| E | HOH230 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 104 |
| Chain | Residue |
| A | C5P102 |
| A | HOH233 |
| A | HOH260 |
| E | C5P101 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 105 |
| Chain | Residue |
| A | C5P102 |
| A | HOH249 |
| B | CTP101 |
| E | HIS57 |
| E | C5P101 |
| E | HOH229 |
| site_id | CC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CDP F 101 |
| Chain | Residue |
| B | CTP101 |
| B | HOH238 |
| C | HIS57 |
| C | C5P102 |
| C | MG103 |
| C | MG104 |
| C | HOH224 |
| D | PHE42 |
| D | TYR55 |
| D | HIS57 |
| D | C5P101 |
| D | MG104 |
| D | MG105 |
| F | GLY4 |
| F | GLN8 |
| F | GLN41 |
| F | PHE42 |
| F | LYS56 |
| F | HIS57 |
| F | NA105 |
| F | HOH212 |
| F | HOH228 |
| F | HOH235 |
| site_id | CC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CTP F 102 |
| Chain | Residue |
| C | ARG19 |
| D | ASN28 |
| D | ILE30 |
| F | TYR25 |
| F | GLY29 |
| F | THR61 |
| F | HOH204 |
| F | HOH213 |
| F | HOH233 |
| F | HOH241 |
| F | HOH249 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL F 103 |
| Chain | Residue |
| D | SER51 |
| D | HOH218 |
| F | PRO67 |
| F | VAL68 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA F 104 |
| Chain | Residue |
| E | GLU18 |
| F | GLU18 |
| F | VAL68 |
| F | ARG69 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA F 105 |
| Chain | Residue |
| B | HOH237 |
| C | C5P102 |
| C | MG104 |
| C | HOH224 |
| D | C5P101 |
| F | CDP101 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 354 |
| Details | Domain: {"description":"Sm","evidences":[{"source":"PROSITE-ProRule","id":"PRU01346","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






