3S4X
Crystal structure of the Asn152Gly mutant of P99 beta-lactamase
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 | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 368 |
| Chain | Residue |
| A | HIS365 |
| A | HIS367 |
| A | HOH593 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 369 |
| Chain | Residue |
| A | HOH558 |
| A | ARG261 |
| A | GLY263 |
| A | TRP276 |
| A | PRO277 |
| A | LYS332 |
| A | HOH499 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 370 |
| Chain | Residue |
| A | VAL211 |
| A | SER212 |
| A | GLY320 |
| A | HIS364 |
| A | HIS365 |
| A | HIS366 |
| A | HOH503 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 371 |
| Chain | Residue |
| A | LYS99 |
| A | LYS183 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 372 |
| Chain | Residue |
| A | PRO18 |
| A | LYS21 |
| A | ARG133 |
| A | ASN137 |
| A | HOH409 |
| A | HOH477 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 A 373 |
| Chain | Residue |
| A | SER64 |
| A | TYR150 |
| A | LYS315 |
| A | THR316 |
| A | GLY317 |
| A | SER318 |
| A | ASN346 |
| A | HIS367 |
| A | HOH420 |
| A | HOH562 |
| A | HOH594 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 374 |
| Chain | Residue |
| A | SER4 |
| A | GLU5 |
| A | HOH509 |
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 | 1 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER64 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR150 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS315 |
Catalytic Information from CSA
| 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 |
