3RES
Crystal structure of E coli Hfq in complex with ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0003723 | molecular_function | RNA binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0003723 | molecular_function | RNA binding |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0003723 | molecular_function | RNA binding |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0003723 | molecular_function | RNA binding |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0003723 | molecular_function | RNA binding |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0003723 | molecular_function | RNA binding |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| H | 0003723 | molecular_function | RNA binding |
| H | 0006355 | biological_process | regulation of DNA-templated transcription |
| I | 0003723 | molecular_function | RNA binding |
| I | 0006355 | biological_process | regulation of DNA-templated transcription |
| J | 0003723 | molecular_function | RNA binding |
| J | 0006355 | biological_process | regulation of DNA-templated transcription |
| K | 0003723 | molecular_function | RNA binding |
| K | 0006355 | biological_process | regulation of DNA-templated transcription |
| L | 0003723 | molecular_function | RNA binding |
| L | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP B 66 |
| Chain | Residue |
| B | TYR25 |
| C | GLN52 |
| B | GLY29 |
| B | LYS31 |
| B | SER60 |
| B | THR61 |
| B | HOH177 |
| C | LEU26 |
| C | ILE30 |
| C | LEU32 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ADP C 66 |
| Chain | Residue |
| C | TYR25 |
| C | GLY29 |
| C | SER60 |
| C | THR61 |
| C | HOH275 |
| D | LEU26 |
| D | ILE30 |
| D | LEU32 |
| D | GLN52 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP E 66 |
| Chain | Residue |
| E | TYR25 |
| E | GLY29 |
| E | LYS31 |
| E | SER60 |
| E | THR61 |
| E | HOH76 |
| F | LEU26 |
| F | ASN28 |
| F | ILE30 |
| F | LEU32 |
| F | GLN41 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP F 66 |
| Chain | Residue |
| A | ASP9 |
| A | LEU26 |
| A | ILE30 |
| A | LEU32 |
| A | GLN52 |
| A | HOH265 |
| F | TYR25 |
| F | GLY29 |
| F | SER60 |
| F | THR61 |
| F | HOH247 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ADP H 66 |
| Chain | Residue |
| H | TYR25 |
| H | GLY29 |
| H | SER60 |
| H | THR61 |
| H | HOH160 |
| I | LEU26 |
| I | ILE30 |
| I | LEU32 |
| I | GLN52 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ADP I 66 |
| Chain | Residue |
| I | ARG16 |
| I | TYR25 |
| I | GLY29 |
| I | SER60 |
| I | THR61 |
| I | HOH266 |
| J | ILE30 |
| J | LEU32 |
| J | GLN52 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP K 66 |
| Chain | Residue |
| K | TYR25 |
| K | GLY29 |
| K | LYS31 |
| K | SER60 |
| K | THR61 |
| K | HOH242 |
| K | HOH260 |
| L | LEU26 |
| L | ASN28 |
| L | ILE30 |
| L | GLN41 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ADP L 66 |
| Chain | Residue |
| G | ASP9 |
| G | LEU26 |
| G | ILE30 |
| G | LEU32 |
| G | GLN52 |
| L | TYR25 |
| L | GLY29 |
| L | SER60 |
| L | THR61 |
