4QY5: Beta-lactamase TEM,Beta-lactamase PSE-4

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.

Method
X-ray diffraction
Resolution
1.5 Å
Organisms
Escherichia coli, Pseudomonas aeruginosa
Chains
1
Atoms
2,487
Mol. weight
29.04 kDa
Ligands
MG
Released
12 Aug 2015

Explore 4QY5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 15 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix27-4014
β-strand43-5081
β-strand56-6051
β-strand66-6722
α-helix69-713
α-helix72-8514
α-helix931
β-strand94-9523
α-helix961
α-helix99-1013
α-helix109-1113
β-strand117-11823
α-helix119-12810
α-helix132-14211
α-helix145-15410
α-helix168-1703
β-strand180-18122
α-helix183-19412
α-helix201-21212
α-helix225-2262
β-strand230-23781
β-strand244-25181
β-strand259-26681
α-helix272-28817

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Beta-lactamase TEM,Beta-lactamase PSE-4Aprotein263Escherichia coli, Pseudomonas aeruginosaP16897 (AlphaFold model), P62593 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4QY5_1 Beta-lactamase TEM,Beta-lactamase PSE-4 (chains A)
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPLTSTFKVLLCGAVLSRVD
AGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP
KELTDFLRQIGDKETRLDRIEPDLNEGKLGDLRDTTTPKAIASTLRKLLTGELLTLASRQ
QLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTG
SQATMDERNRQIAEIGASLIKHW

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg3

Water and common crystallization additives (CL) are not listed.

Primary citation

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:

Browse structure collections

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