1NYM
Crystal Structure of the complex between M182T mutant of TEM-1 and a boronic acid inhibitor (CXB)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 1000 |
| Chain | Residue |
| A | LEU57 |
| A | GLU58 |
| A | ASN100 |
| A | HOH1653 |
| A | HOH1673 |
| A | HOH1705 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1001 |
| Chain | Residue |
| A | HOH1640 |
| A | HOH1690 |
| A | TYR97 |
| A | LEU113 |
| A | HOH1593 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 1003 |
| Chain | Residue |
| A | MET211 |
| A | ALA213 |
| A | ASP214 |
| A | ASP233 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1501 |
| Chain | Residue |
| A | ASP115 |
| A | ARG275 |
| A | CXB300 |
| A | HOH1518 |
| A | HOH1522 |
| A | HOH1534 |
| A | HOH1551 |
| A | HOH1564 |
| A | HOH1633 |
| A | HOH1675 |
| A | HOH1738 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1502 |
| Chain | Residue |
| A | LEU91 |
| A | GLY92 |
| A | ARG120 |
| A | HOH1608 |
| A | HOH1897 |
| A | HOH1899 |
| A | HOH1905 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CXB A 300 |
| Chain | Residue |
| A | MET69 |
| A | SER70 |
| A | LYS73 |
| A | TYR105 |
| A | SER130 |
| A | ASN132 |
| A | GLY236 |
| A | ALA237 |
| A | GLY238 |
| A | GLU240 |
| A | PO41501 |
| A | HOH1571 |
| A | HOH1624 |
| A | HOH1633 |
| A | HOH1636 |
| A | HOH1898 |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL |
| Chain | Residue | Details |
| A | PHE66-LEU81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Acyl-ester intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | GLU166 | |
| A | LYS73 | |
| A | SER130 | |
| A | SER70 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| A | SER70 | electrostatic stabiliser |
| A | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS234 | electrostatic stabiliser |
| A | ALA237 | electrostatic stabiliser, hydrogen bond donor |
