5US8
2.15 Angstrom Resolution Crystal Structure of Argininosuccinate Synthase from Bordetella pertussis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000050 | biological_process | urea cycle |
| A | 0000053 | biological_process | argininosuccinate metabolic process |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004055 | molecular_function | argininosuccinate synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000050 | biological_process | urea cycle |
| B | 0000053 | biological_process | argininosuccinate metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004055 | molecular_function | argininosuccinate synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue EPE A 501 |
| Chain | Residue |
| A | TYR254 |
| A | ALA255 |
| A | ASP256 |
| A | HOH728 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue PGE A 502 |
| Chain | Residue |
| A | GLY180 |
| A | ARG270 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EPE B 501 |
| Chain | Residue |
| B | TYR254 |
| B | ALA255 |
| B | ASP256 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EPE B 502 |
| Chain | Residue |
| B | GLY21 |
| B | LEU22 |
| B | GLN47 |
| B | ASP49 |
| B | GLU50 |
| B | ARG169 |
| B | TYR183 |
| B | SER186 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue ADN B 503 |
| Chain | Residue |
| A | GLU318 |
| A | GLU322 |
| A | ARG325 |
| A | LYS326 |
| B | ARG321 |
| B | GLU322 |
| B | ARG325 |
| B | LYS326 |
| B | HOH601 |
| B | HOH678 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | HOH694 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00581","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
