6BXL
Crystal structure of Pyrococcus horikoshii Dph2 with 4Fe-4S cluster and SAM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0017183 | biological_process | protein histidyl modification to diphthamide |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050843 | biological_process | S-adenosylmethionine catabolic process |
| 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 | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0017183 | biological_process | protein histidyl modification to diphthamide |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050843 | biological_process | S-adenosylmethionine catabolic process |
| 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 | 14 |
| Details | binding site for residue SAM A 401 |
| Chain | Residue |
| A | TYR56 |
| A | CYS287 |
| A | ARG289 |
| A | VAL290 |
| A | ASP293 |
| A | SF4402 |
| A | LEU161 |
| A | GLY162 |
| A | HIS184 |
| A | LYS238 |
| A | GLN241 |
| A | ASN267 |
| A | ASP268 |
| A | VAL269 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 A 402 |
| Chain | Residue |
| A | TYR56 |
| A | CYS59 |
| A | GLY162 |
| A | CYS163 |
| A | GLN241 |
| A | CYS287 |
| A | SAM401 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue SAM B 401 |
| Chain | Residue |
| B | TYR56 |
| B | LEU161 |
| B | GLY162 |
| B | HIS184 |
| B | LYS238 |
| B | GLN241 |
| B | ASN267 |
| B | ASP268 |
| B | VAL269 |
| B | CYS287 |
| B | ARG289 |
| B | SF4402 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 B 402 |
| Chain | Residue |
| B | TYR56 |
| B | CYS59 |
| B | ARG153 |
| B | GLY162 |
| B | CYS163 |
| B | CYS287 |
| B | ARG289 |
| B | SAM401 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SriswpgqvlGcnYSVAKVRGeGILfIGS |
| Chain | Residue | Details |
| A | SER152-SER180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS59 | |
| A | CYS163 | |
| A | CYS287 | |
| B | CYS59 | |
| B | CYS163 | |
| B | CYS287 |
