2AE3
Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
A | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 301 |
Chain | Residue |
A | LEU148 |
A | SER152 |
A | PRO162 |
A | HOH324 |
B | PHE31 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
B | SER1 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255 |
Chain | Residue | Details |
B | HIS23 | |
B | GLU455 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 3s8r |
Chain | Residue | Details |
B | SER1 | |
B | ASN244 | |
B | VAL70 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 288 |
Chain | Residue | Details |
B | SER1 | activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
B | HIS23 | activator, electrostatic stabiliser, increase acidity, steric role |
B | VAL70 | electrostatic stabiliser |
B | ASN244 | electrostatic stabiliser |
B | GLU455 | activator, electrostatic stabiliser, increase acidity, steric role |