3S8R
Crystal Structures of Glutaryl 7-Aminocephalosporanic Acid Acylase: Insight into Autoproteolytic Activation
Replaces: 1OQZFunctional 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 |
| A | 0033968 | molecular_function | glutaryl-7-aminocephalosporanic-acid acylase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0033968 | molecular_function | glutaryl-7-aminocephalosporanic-acid acylase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 698 |
| Chain | Residue |
| A | THR76 |
| A | LEU148 |
| A | PRO153 |
| A | ASP164 |
| A | TYR199 |
| A | HOH813 |
| A | HOH893 |
| A | HOH1021 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 698 |
| Chain | Residue |
| B | ARG143 |
| B | LEU148 |
| B | TYR199 |
| B | HOH746 |
| B | HOH938 |
| B | THR76 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | ALA170 | |
| B | ALA170 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| A | HIS192 | |
| A | GLU624 | |
| B | HIS192 | |
| B | GLU624 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11080627, 11755403 |
| Chain | Residue | Details |
| A | SER170 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 288 |
| Chain | Residue | Details |
| A | ALA170 | activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| A | HIS192 | activator, electrostatic stabiliser, increase acidity, steric role |
| A | VAL239 | electrostatic stabiliser |
| A | ASN413 | electrostatic stabiliser |
| A | GLU624 | activator, electrostatic stabiliser, increase acidity, steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 288 |
| Chain | Residue | Details |
| B | ALA170 | activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| B | HIS192 | activator, electrostatic stabiliser, increase acidity, steric role |
| B | VAL239 | electrostatic stabiliser |
| B | ASN413 | electrostatic stabiliser |
| B | GLU624 | activator, electrostatic stabiliser, increase acidity, steric role |
