4RHM
Crystal structure of T. brucei arginase-like protein quadruple mutant S149D/R151H/S153D/S226D
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004053 | molecular_function | arginase activity |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0008783 | molecular_function | agmatinase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004053 | molecular_function | arginase activity |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0008783 | molecular_function | agmatinase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004053 | molecular_function | arginase activity |
| C | 0006525 | biological_process | arginine metabolic process |
| C | 0008783 | molecular_function | agmatinase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 401 |
| Chain | Residue |
| A | ARG38 |
| A | PRO40 |
| A | TYR269 |
| A | ASN280 |
| A | GLY282 |
| A | ALA285 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 402 |
| Chain | Residue |
| A | ASP226 |
| A | HOH511 |
| A | ASP149 |
| A | HIS151 |
| A | ASP224 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | PRO239 |
| A | VAL240 |
| A | ALA241 |
| A | HOH514 |
| B | SER48 |
| B | ILE286 |
| B | SER289 |
| B | LYS293 |
| B | HOH511 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 404 |
| Chain | Residue |
| A | GLY243 |
| A | SER245 |
| A | ASP248 |
| B | SER245 |
| B | ASP248 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 401 |
| Chain | Residue |
| B | TYR269 |
| B | TYR276 |
| B | ASN280 |
| B | GLY282 |
| B | ALA285 |
| B | HOH508 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 402 |
| Chain | Residue |
| B | ASP149 |
| B | HIS151 |
| B | ASP224 |
| B | ASP226 |
| B | HOH513 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 403 |
| Chain | Residue |
| B | GLY243 |
| B | SER245 |
| B | ASP248 |
| C | SER245 |
| C | ASP248 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 401 |
| Chain | Residue |
| A | SER48 |
| A | ILE286 |
| A | SER289 |
| A | LYS290 |
| A | LYS293 |
| C | PRO239 |
| C | VAL240 |
| C | ALA241 |
| C | HOH502 |
| C | HOH522 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 402 |
| Chain | Residue |
| A | SER245 |
| A | ASP248 |
| C | GLY243 |
| C | SER245 |
| C | ASP248 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 403 |
| Chain | Residue |
| C | TYR269 |
| C | ASN280 |
| C | GLY282 |
| C | ALA285 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 404 |
| Chain | Residue |
| C | ASP149 |
| C | HIS151 |
| C | ASP224 |
| C | ASP226 |
| C | HOH516 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 405 |
| Chain | Residue |
| B | PRO239 |
| B | VAL240 |
| B | ALA241 |
| C | SER48 |
| C | ILE286 |
| C | SER289 |
| C | LYS293 |
| C | HOH509 |
