4ID4: Chimeric beta-lactamase cTEM-17m

Crystal structure of chimeric beta-lactamase cTEM-17m. Determined by X-ray diffraction at 1.05 Å resolution. Released 25 Dec 2013.

Method
X-ray diffraction
Resolution
1.05 Å
Organisms
Escherichia coli, Pseudomonas aeruginosa
Chains
1
Atoms
2,691
Mol. weight
29.08 kDa
Ligands
MG
Released
25 Dec 2013

Explore 4ID4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ID4 contains 13 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: 13 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix27-4014
β-strand43-5081
β-strand56-6051
β-strand66-6722
α-helix69-713
α-helix72-8514
β-strand94-9523
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
>4ID4_1 Beta-lactamase TEM, Beta-lactamase PSE-4 (chains A)
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVD
AGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP
KELTDFLRQIGDKETRLDRIEPDLNEGKLGDLRDTTTPKAIASTLRKLLTGELLTLASRQ
QLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTG
SQATMDERNRQIAEIGASLIKHW

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

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

Primary citation

Maintenance of Native-like Protein Dynamics May Not Be Required for Engineering Functional Proteins. Gobeil, S.M., Clouthier, C.M., Park, J. et al. Chem Biol (2014) 21:1330-1340. DOI 10.1016/j.chembiol.2014.07.016 · PubMed

Other PDB entries of the same protein (UniProt P16897 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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