1OR0
Crystal Structures of Glutaryl 7-Aminocephalosporanic Acid Acylase: Insight into Autoproteolytic Activation
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 |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO B 2001 |
| Chain | Residue |
| A | HOH318 |
| B | PHE177 |
| B | HOH2389 |
| B | SER1 |
| B | PRO22 |
| B | TYR33 |
| B | ARG57 |
| B | PHE58 |
| B | ASN68 |
| B | THR69 |
| B | VAL70 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 2002 |
| Chain | Residue |
| D | SER1 |
| D | ARG57 |
| D | PHE58 |
| D | ASN68 |
| D | THR69 |
| D | PHE177 |
| D | HOH2458 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3s8r |
| Chain | Residue | Details |
| B | SER1 | |
| B | ASN244 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3s8r |
| Chain | Residue | Details |
| D | SER1 | |
| D | ASN244 |
| 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 | VAL74 | electrostatic stabiliser |
| B | TYR264 | electrostatic stabiliser |
| B | GLU491 | activator, electrostatic stabiliser, increase acidity, steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 288 |
| Chain | Residue | Details |
| D | SER1 | activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| D | HIS23 | activator, electrostatic stabiliser, increase acidity, steric role |
| D | VAL74 | electrostatic stabiliser |
| D | TYR264 | electrostatic stabiliser |
| D | GLU491 | activator, electrostatic stabiliser, increase acidity, steric role |
