4XUX
Structure of ampC bound to RPX-7009 at 1.75 A
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue 4D6 A 401 |
| Chain | Residue |
| A | SER84 |
| A | ASN366 |
| A | HOH711 |
| A | GLN140 |
| A | TYR170 |
| A | ASN172 |
| A | TYR241 |
| A | THR336 |
| A | GLY337 |
| A | SER338 |
| A | GLY340 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | GLU292 |
| A | HIS334 |
| A | LYS335 |
| A | THR336 |
| A | HOH663 |
| A | HOH670 |
| A | HOH729 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | GLN161 |
| A | ASP265 |
| A | HOH511 |
| A | HOH548 |
| A | HOH728 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue PG0 A 404 |
| Chain | Residue |
| A | TRP113 |
| A | ASN148 |
| A | ALA180 |
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 | PHE80-LYS87 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER84 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR170 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS335 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 257 |
| Chain | Residue | Details |
| A | SER84 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS87 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| A | TYR170 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU292 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS335 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| A | SER338 | electrostatic stabiliser, hydrogen bond donor |
