2E9F
Crystal Structure of T.th.HB8 Argininosuccinate lyase complexed with L-Arginine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004056 | molecular_function | argininosuccinate lyase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | arginine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004056 | molecular_function | argininosuccinate lyase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | arginine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004056 | molecular_function | argininosuccinate lyase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006526 | biological_process | arginine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004056 | molecular_function | argininosuccinate lyase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006526 | biological_process | arginine biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0042450 | biological_process | arginine biosynthetic process via ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ARG B 491 |
| Chain | Residue |
| A | HIS159 |
| B | ASP84 |
| B | ARG110 |
| B | ASN111 |
| B | VAL114 |
| B | TYR320 |
| B | GLN325 |
| B | LYS328 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ARG B 492 |
| Chain | Residue |
| A | ARG110 |
| A | ASN111 |
| A | VAL114 |
| A | TYR320 |
| A | GLN325 |
| A | LYS328 |
| B | HIS159 |
| A | SER24 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ARG B 493 |
| Chain | Residue |
| C | HIS159 |
| D | ASN111 |
| D | VAL114 |
| D | TYR320 |
| D | GLN325 |
| D | LYS328 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ARG B 494 |
| Chain | Residue |
| B | HOH1106 |
| C | ASP84 |
| C | ARG110 |
| C | ASN111 |
| C | VAL114 |
| C | TYR320 |
| C | GLN325 |
| C | LYS328 |
| D | HIS159 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSsiMpQKkN |
| Chain | Residue | Details |
| A | GLY279-ASN288 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | THR158 | |
| A | HIS159 | |
| C | SER280 | |
| C | LYS286 | |
| C | GLU293 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| D | SER280 | |
| D | LYS286 | |
| D | GLU293 | |
| B | THR158 | |
| B | HIS159 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | SER280 | |
| A | LYS286 | |
| A | GLU293 | |
| C | THR158 | |
| C | HIS159 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| D | THR158 | |
| D | HIS159 | |
| B | SER280 | |
| B | LYS286 | |
| B | GLU293 |
