1M40: Ultra high resolution crystal structure of tem-1

Ultra high resolution crystal structure of tem-1. Determined by X-ray diffraction at 0.85 Å resolution. Released 17 Jul 2002.

Method: X-ray diffraction
Resolution: 0.85 Å
Organism: Escherichia coli
Chains: 1
Atoms: 3,969
Mol. weight: 29.68 kDa
Ligands: CB4, PO4
Released: 17 Jul 2002

Explore 1M40 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M40 contains 17 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: 17 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	27-40	14
β-strand	44-50	7	1
β-strand	56-60	5	1
β-strand	66-67	2	2
α-helix	69-71	3
α-helix	72-86	15
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	221-224	4
α-helix	225-226	2
β-strand	230-237	8	1
β-strand	244-251	8	1
α-helix	252-255	3
β-strand	259-265	7	1
α-helix	272-288	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-lactamase tem	A	protein	263	Escherichia coli	P62593 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1M40_1 BETA-LACTAMASE TEM (chains A)
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVD
AGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP
KELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTTPAAMATTLRKLLTGELLTLASRQ
QLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTG
SQATMDERNRQIAEIGASLIKHW

Ligands and cofactors

ID	Name	Formula	Copies
CB4	PINACOL[[2-amino-alpha-(1-carboxy-1-methylethoxyimino)-4-thiazoleacetyl]amino]m…	C10 H15 B N4 O6 S	1
PO4	Phosphate ion	O4 P	3

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

Primary citation

An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation. Minasov, G., Wang, X., Shoichet, B.K. J Am Chem Soc (2002) 124:5333-5340. DOI 10.1021/ja0259640 · PubMed

Other PDB entries of the same protein (UniProt P62593 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ID4 1.05 Å, Crystal structure of chimeric beta-lactamase cTEM-17m
4R4S 1.1 Å, Crystal structure of chimeric beta-lactamase cTEM-19m at 1.1 angstrom resolution
4QY6 1.15 Å, Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations
1NYM 1.2 Å, Crystal Structure of the complex between M182T mutant of TEM-1 and a boronic acid…
4R4R 1.2 Å, Crystal structure of chimeric beta-lactamase cTEM-19m at 1.2 angstrom resolution
4RX3 1.39 Å, A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile…
1YT4 1.4 Å, Crystal structure of TEM-76 beta-lactamase at 1.4 Angstrom resolution
5HW5 1.41 Å, Crystal structure of TEM1 beta-lactamase in the presence of 2.0 MPa xenon
4RVA 1.44 Å, A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile…
6AYK 1.44 Å, Crystal structure of TEM1 beta-lactamase mutant I263A in the presence of 1.2 MPa xenon
1PZP 1.45 Å, TEM-1 Beta-Lactamase in Complex with a Novel, Core-Disrupting, Allosteric Inhibitor
8DDZ 1.45 Å, TEM-1 beta-lactamase A237Y

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