2AAF
Structure of H278A arginine deiminase with L-arginine forming a S-alkylthiouronium reaction intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0016990 | molecular_function | arginine deiminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0016990 | molecular_function | arginine deiminase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006527 | biological_process | L-arginine catabolic process |
| C | 0016990 | molecular_function | arginine deiminase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006527 | biological_process | L-arginine catabolic process |
| D | 0016990 | molecular_function | arginine deiminase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. VETGGNSF |
| Chain | Residue | Details |
| A | VAL341-PHE348 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Amidino-cysteine intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






