2PFM
Crystal Structure of Adenylosuccinate Lyase (PurB) from Bacillus anthracis
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 | 0005737 | cellular_component | cytoplasm |
| 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 | 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 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 | 11 |
| Details | BINDING SITE FOR RESIDUE MLI A 901 |
| Chain | Residue |
| A | THR142 |
| B | ASN272 |
| B | HOH649 |
| A | HIS143 |
| B | HIS68 |
| B | SER96 |
| B | GLN214 |
| B | GLY263 |
| B | SER264 |
| B | MET267 |
| B | LYS270 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLI A 902 |
| Chain | Residue |
| A | HIS68 |
| A | SER96 |
| A | GLN214 |
| A | GLY263 |
| A | SER264 |
| A | MET267 |
| A | LYS270 |
| A | ASN272 |
| B | THR142 |
| B | HIS143 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MLI A 903 |
| Chain | Residue |
| A | GLN110 |
| A | HOH951 |
| A | HOH991 |
| A | HOH1090 |
| B | HOH616 |
| B | HOH634 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSsaMpHKrN |
| Chain | Residue | Details |
| A | GLY263-ASN272 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | SER264 | |
| A | GLU277 | |
| A | LYS270 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| B | THR142 | |
| B | HIS143 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| B | SER264 | |
| B | GLU277 | |
| B | LYS270 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | THR142 | |
| A | HIS143 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | GLU277 | |
| A | LYS270 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| B | GLU277 | |
| B | LYS270 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| B | HIS143 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | HIS143 |
