6EWZ
Crystal structure of RelP (SAS2) from Staphylococcus aureus bound to AMPCPP and GTP in the pre-catalytic state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0008728 | molecular_function | GTP diphosphokinase activity |
| A | 0015969 | biological_process | guanosine tetraphosphate metabolic process |
| A | 0015970 | biological_process | guanosine tetraphosphate biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0008728 | molecular_function | GTP diphosphokinase activity |
| B | 0015969 | biological_process | guanosine tetraphosphate metabolic process |
| B | 0015970 | biological_process | guanosine tetraphosphate biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue GTP A 301 |
| Chain | Residue |
| A | LYS88 |
| A | GLU174 |
| A | GLN176 |
| A | ALA186 |
| A | GLU189 |
| A | ARG193 |
| A | APC302 |
| A | MG303 |
| A | HOH406 |
| A | HOH407 |
| A | HOH413 |
| A | LYS92 |
| A | HOH424 |
| A | HOH449 |
| A | LYS138 |
| A | LYS140 |
| A | TYR142 |
| A | LYS147 |
| A | ASN149 |
| A | TYR151 |
| A | HIS155 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue APC A 302 |
| Chain | Residue |
| A | GLU76 |
| A | ARG78 |
| A | LYS80 |
| A | SER84 |
| A | LYS88 |
| A | ARG91 |
| A | ASP107 |
| A | GLY110 |
| A | ILE111 |
| A | ARG112 |
| A | GLU174 |
| A | GLN176 |
| A | GTP301 |
| A | MG303 |
| A | HOH424 |
| A | HOH425 |
| A | HOH441 |
| A | HOH446 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | LYS80 |
| A | LYS88 |
| A | ASP107 |
| A | GTP301 |
| A | APC302 |
| A | HOH406 |
| A | HOH424 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue FE A 304 |
| Chain | Residue |
| A | GLU51 |
| A | HOH419 |
| A | HOH433 |
| A | HOH436 |
| A | HOH444 |
| B | GLU51 |
| B | HOH405 |
| B | HOH414 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue GTP B 301 |
| Chain | Residue |
| B | LYS88 |
| B | LYS92 |
| B | LYS138 |
| B | TYR142 |
| B | LYS147 |
| B | ASN149 |
| B | TYR151 |
| B | HIS155 |
| B | GLU174 |
| B | GLN176 |
| B | ALA186 |
| B | GLU189 |
| B | HIS190 |
| B | APC302 |
| B | MG303 |
| B | HOH401 |
| B | HOH412 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue APC B 302 |
| Chain | Residue |
| B | GLU76 |
| B | ARG78 |
| B | LYS80 |
| B | SER84 |
| B | LYS88 |
| B | ARG91 |
| B | ASP107 |
| B | GLY110 |
| B | ILE111 |
| B | ARG112 |
| B | GLU174 |
| B | GLN176 |
| B | HIS190 |
| B | GTP301 |
| B | MG303 |
| B | HOH412 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| B | LYS80 |
| B | LYS88 |
| B | ASP107 |
| B | GTP301 |
| B | APC302 |
| B | HOH401 |
| B | HOH412 |
