1BLS
CRYSTALLOGRAPHIC STRUCTURE OF A PHOSPHONATE DERIVATIVE OF THE ENTEROBACTER CLOACAE P99 CEPHALOSPORINASE: MECHANISTIC INTERPRETATION OF A BETA-LACTAMASE TRANSITION STATE ANALOG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IPP A 362 |
| Chain | Residue |
| A | SER64 |
| A | GLN120 |
| A | TYR150 |
| A | ASN152 |
| A | TYR221 |
| A | GLY317 |
| A | SER318 |
| A | GLY320 |
| A | HOH563 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IPP B 362 |
| Chain | Residue |
| B | SER64 |
| B | GLN120 |
| B | TYR150 |
| B | ASN152 |
| B | TYR221 |
| B | GLY317 |
| B | SER318 |
| B | HOH480 |
| B | HOH657 |
Functional Information from PROSITE/UniProt
| site_id | PS00336 |
| Number of Residues | 8 |
| Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSISK |
| Chain | Residue | Details |
| A | PHE60-LYS67 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER64 | |
| B | SER64 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR150 | |
| B | TYR150 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS315 | |
| B | LYS315 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1xx2 |
| Chain | Residue | Details |
| A | GLU272 | |
| A | SER64 | |
| A | LYS315 | |
| A | TYR150 | |
| A | LYS67 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1xx2 |
| Chain | Residue | Details |
| B | GLU272 | |
| B | SER64 | |
| B | LYS315 | |
| B | TYR150 | |
| B | LYS67 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 257 |
| Chain | Residue | Details |
| A | SER64 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS67 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| A | TYR150 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU272 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS315 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| A | SER318 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 257 |
| Chain | Residue | Details |
| B | SER64 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS67 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| B | TYR150 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU272 | electrostatic stabiliser, hydrogen bond acceptor |
| B | LYS315 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| B | SER318 | electrostatic stabiliser, hydrogen bond donor |
