3DTM
Increased folding stability of TEM-1 beta-lactamase by in-vitro selection
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | Beta-lactamase | polymer | 263 | 28857.9 | 1 | UniProt (Q79DR3) Pfam (PF00144) Pfam (PF13354) UniProt (by SIFTS) (P62593) In PDB | Escherichia coli | Extended spectrum beta-lactamase, TEM extended spectrum beta-lactamase, Betalactamase TEM-116, Mutant extended-spectrum beta-lactamase precursor, Beta lactamase precursor |
| 2 | water | water | 18.0 | 120 | Chemie (HOH) |
Sequence modifications
A: 26 - 288 (UniProt: Q79DR3)
| PDB | External Database | Details |
|---|---|---|
| Ser 62 | Pro 60 | engineered mutation |
| Ile 80 | Val 78 | engineered mutation |
| Gly 147 | Glu 145 | engineered mutation |
| Thr 182 | Met 180 | engineered mutation |
| Pro 201 | Leu 199 | engineered mutation |
| Met 208 | Ile 206 | engineered mutation |
| Val 224 | Ala 222 | engineered mutation |
| Val 246 | Ile 244 | engineered mutation |
| Leu 273 | Arg 271 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 28857.9 | |
| All* | Total formula weight | 28857.9 |
