6Q2E
Crystal structure of Methanobrevibacter smithii Dph2 bound to 5'-methylthioadenosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017183 | biological_process | protein histidyl modification to diphthamide |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0090560 | molecular_function | 2-(3-amino-3-carboxypropyl)histidine synthase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017183 | biological_process | protein histidyl modification to diphthamide |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0090560 | molecular_function | 2-(3-amino-3-carboxypropyl)histidine synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue MTA A 401 |
| Chain | Residue |
| A | PHE58 |
| A | ASP296 |
| A | HOH568 |
| A | HOH702 |
| A | LYS239 |
| A | GLN242 |
| A | ASP268 |
| A | ASN269 |
| A | ILE270 |
| A | CYS289 |
| A | ARG291 |
| A | ASP295 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SF4 A 402 |
| Chain | Residue |
| A | PHE58 |
| A | CYS61 |
| A | GLY160 |
| A | CYS161 |
| A | CYS289 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | MET245 |
| A | LYS246 |
| A | HOH788 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue MTA B 401 |
| Chain | Residue |
| B | PHE58 |
| B | SER237 |
| B | LYS239 |
| B | GLN242 |
| B | ASP268 |
| B | ASN269 |
| B | ILE270 |
| B | CYS289 |
| B | ARG291 |
| B | ILE292 |
| B | ASP295 |
| B | ASP296 |
| B | HOH607 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SF4 B 402 |
| Chain | Residue |
| B | PHE58 |
| B | CYS61 |
| B | GLY160 |
| B | CYS161 |
| B | CYS289 |
