5VKW
Crystal structure of adenylosuccinate lyase ADE13 from Candida albicans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | THR108 |
| A | ARG193 |
| A | LYS196 |
| A | GLY197 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| B | GLN161 |
| A | GLY197 |
| A | THR198 |
| A | ALA203 |
| A | SER204 |
| A | HOH743 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | ARG300 |
| A | HOH762 |
| B | HOH867 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 505 |
| Chain | Residue |
| A | ASP417 |
| A | ASP417 |
| A | HOH677 |
| A | HOH677 |
| A | HOH1012 |
| A | HOH1012 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 501 |
| Chain | Residue |
| B | THR108 |
| B | PHE111 |
| B | ARG193 |
| B | LYS196 |
| B | GLY197 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| A | GLN161 |
| B | GLY197 |
| B | THR198 |
| B | ALA203 |
| B | SER204 |
| B | HOH800 |
| B | HOH932 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | THR67 |
| B | ASP68 |
| B | HOH1111 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| A | HOH847 |
| B | ARG300 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| B | GLU225 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 507 |
| Chain | Residue |
| A | ASP436 |
| A | HOH747 |
| A | HOH999 |
| B | ASP214 |
| B | HOH942 |
| B | HOH962 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 508 |
| Chain | Residue |
| B | ASP54 |
| B | GLU58 |
| B | HOH730 |
| B | HOH947 |
| B | HOH969 |
| B | HOH978 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue PGE B 509 |
| Chain | Residue |
| B | GLU145 |
| B | TYR146 |
| B | ASP148 |
| B | LEU149 |
| B | HOH737 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 510 |
| Chain | Residue |
| B | ASN435 |
| B | ASN435 |
| B | ASP438 |
| B | ASP438 |
| B | HOH928 |
| B | HOH928 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSsaMaYKrN |
| Chain | Residue | Details |
| A | GLY285-ASN294 |
