1BTL
CRYSTAL STRUCTURE OF ESCHERICHIA COLI TEM1 BETA-LACTAMASE AT 1.8 ANGSTROMS RESOLUTION
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 291 |
| Chain | Residue |
| A | SER70 |
| A | SER130 |
| A | SER235 |
| A | GLY236 |
| A | ARG244 |
| A | HOH323 |
| A | HOH437 |
| site_id | ACT |
| Number of Residues | 11 |
| Details |
| Chain | Residue |
| A | SER70 |
| A | GLY238 |
| A | ARG244 |
| A | LYS73 |
| A | SER130 |
| A | ASN132 |
| A | GLU166 |
| A | LYS234 |
| A | SER235 |
| A | GLY236 |
| A | ALA237 |
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":"Nucleophile; acyl-ester intermediate","evidences":[{"source":"PubMed","id":"9485412","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9485412","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9485412","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | a catalytic site defined by CSA, PubMed 1930139, 8700829, 12904016, 10716727, 1436034, 8823158 |
| Chain | Residue | Details |
| A | SER70 | |
| A | SER70 | |
| A | GLU166 | |
| A | SER130 | |
| A | LYS73 | |
| A | LYS234 | |
| A | ALA237 |
| 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 |
