3SY8
Crystal structure of the response regulator RocR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071111 | molecular_function | cyclic-guanylate-specific phosphodiesterase activity |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071111 | molecular_function | cyclic-guanylate-specific phosphodiesterase activity |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071111 | molecular_function | cyclic-guanylate-specific phosphodiesterase activity |
| D | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071111 | molecular_function | cyclic-guanylate-specific phosphodiesterase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | GLU175 |
| A | ASN233 |
| A | GLU265 |
| A | ASP295 |
| A | HOH410 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | GLU175 |
| B | ASN233 |
| B | GLU265 |
| B | ASP295 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 401 |
| Chain | Residue |
| C | GLU175 |
| C | ASN233 |
| C | GLU265 |
| C | ASP295 |
| C | HOH417 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 401 |
| Chain | Residue |
| D | GLU175 |
| D | ASN233 |
| D | GLU265 |
| D | ASP295 |
| D | EPE3380 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE EPE D 3380 |
| Chain | Residue |
| A | GLU116 |
| D | GLN161 |
| D | GLU175 |
| D | LEU177 |
| D | ASN233 |
| D | ASP295 |
| D | GLU352 |
| D | GLY353 |
| D | GLN372 |
| D | GLY373 |
| D | TYR374 |
| D | MG401 |
| D | HOH405 |
| D | HOH417 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:18344366 |
| Chain | Residue | Details |
| A | GLU352 | |
| B | GLU352 | |
| C | GLU352 | |
| D | GLU352 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22753070, ECO:0007744|PDB:3SY8 |
| Chain | Residue | Details |
| A | GLU175 | |
| C | ASN233 | |
| C | GLU265 | |
| C | ASP295 | |
| D | GLU175 | |
| D | ASN233 | |
| D | GLU265 | |
| D | ASP295 | |
| A | ASN233 | |
| A | GLU265 | |
| A | ASP295 | |
| B | GLU175 | |
| B | ASN233 | |
| B | GLU265 | |
| B | ASP295 | |
| C | GLU175 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169 |
| Chain | Residue | Details |
| A | ASP56 | |
| B | ASP56 | |
| C | ASP56 | |
| D | ASP56 |
