5EY1
Crystal structure of CodY from Staphylococcus aureus with GTP and Ile
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000976 | molecular_function | transcription cis-regulatory region binding |
| A | 0001217 | molecular_function | DNA-binding transcription repressor activity |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0032993 | cellular_component | protein-DNA complex |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000976 | molecular_function | transcription cis-regulatory region binding |
| B | 0001217 | molecular_function | DNA-binding transcription repressor activity |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0032993 | cellular_component | protein-DNA complex |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue ILE A 301 |
| Chain | Residue |
| A | ARG61 |
| A | HOH485 |
| A | MET65 |
| A | THR96 |
| A | VAL97 |
| A | PHE98 |
| A | PRO99 |
| A | PRO100 |
| A | HOH440 |
| A | HOH462 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue GTP A 302 |
| Chain | Residue |
| A | VAL22 |
| A | ASP23 |
| A | PHE24 |
| A | SER43 |
| A | ARG44 |
| A | ARG45 |
| A | LYS47 |
| A | LEU49 |
| A | GLU153 |
| A | ILE154 |
| A | ARG156 |
| A | GLU157 |
| A | LYS158 |
| A | GLU161 |
| A | HOH401 |
| A | HOH410 |
| A | HOH447 |
| A | HOH449 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue ILE B 301 |
| Chain | Residue |
| B | ARG61 |
| B | PRO72 |
| B | TYR75 |
| B | THR96 |
| B | VAL97 |
| B | PHE98 |
| B | PRO100 |
| B | HOH435 |
| B | HOH442 |
| B | HOH462 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue GTP B 302 |
| Chain | Residue |
| A | TYR181 |
| B | VAL22 |
| B | PHE24 |
| B | SER43 |
| B | ARG44 |
| B | ARG45 |
| B | LYS47 |
| B | LEU49 |
| B | GLU153 |
| B | GLU157 |
| B | LYS158 |
| B | HOH415 |
| B | HOH419 |
| B | HOH423 |
| B | HOH463 |
| B | HOH472 |
| B | HOH473 |
| B | HOH477 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 308 |
| Details | Region: {"description":"GAF domain","evidences":[{"source":"HAMAP-Rule","id":"MF_00621","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27596595","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EY0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5EY1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
