Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations. Determined by X-ray diffraction at 1.5 Å resolution. Released 12 Aug 2015.
Explore 4QY5 in 3D Show helices and sheets RCSB PDB PDBe
4QY5 contains 15 α-helices and 9 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-40 | 14 | |
| β-strand | 43-50 | 8 | 1 |
| β-strand | 56-60 | 5 | 1 |
| β-strand | 66-67 | 2 | 2 |
| α-helix | 69-71 | 3 | |
| α-helix | 72-85 | 14 | |
| α-helix | 93 | 1 | |
| β-strand | 94-95 | 2 | 3 |
| α-helix | 96 | 1 | |
| α-helix | 99-101 | 3 | |
| α-helix | 109-111 | 3 | |
| β-strand | 117-118 | 2 | 3 |
| α-helix | 119-128 | 10 | |
| α-helix | 132-142 | 11 | |
| α-helix | 145-154 | 10 | |
| α-helix | 168-170 | 3 | |
| β-strand | 180-181 | 2 | 2 |
| α-helix | 183-194 | 12 | |
| α-helix | 201-212 | 12 | |
| α-helix | 225-226 | 2 | |
| β-strand | 230-237 | 8 | 1 |
| β-strand | 244-251 | 8 | 1 |
| β-strand | 259-266 | 8 | 1 |
| α-helix | 272-288 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-lactamase TEM,Beta-lactamase PSE-4 | A | protein | 263 | Escherichia coli, Pseudomonas aeruginosa | P16897 (AlphaFold model), P62593 (AlphaFold model) |
>4QY5_1 Beta-lactamase TEM,Beta-lactamase PSE-4 (chains A) HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPLTSTFKVLLCGAVLSRVD AGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP KELTDFLRQIGDKETRLDRIEPDLNEGKLGDLRDTTTPKAIASTLRKLLTGELLTLASRQ QLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTG SQATMDERNRQIAEIGASLIKHW
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 3 |
Water and common crystallization additives (CL) are not listed.
Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations. Park, J., Gobeil, S., Pelletier, J.N. et al. To be published.
Other PDB entries of the same protein (UniProt P16897 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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