Escherichia coli · seed P62593 · 286 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P62593 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.40.710.10 CATH 3.40.190.10 SCOP 8041576 SCOP 8038399 SCOP 8069801 SCOP 8069815 SCOP 8037342 SCOP 8069805 SCOP 8069809 SCOP 8069821 SCOP 8069779 SCOP 8069823 SCOP 8035959 SCOP 8037344 SCOP 8069867 SCOP 8104351 RCSB 1LHY PDBe
CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.
Every figure here is counted over the whole family rather than quoted from one entry.
1LHY, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.
How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.
337 distinct constructs across 769 entries. 655 polymer entities differ from the UniProt canonical sequence in some way, 93 carry a recognised expression tag and 3 carry a fusion partner.
"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.
| Entities | Length | Best (Å) | Best entry | What was made |
|---|---|---|---|---|
| 48 | 263 | 0.79 | 4UA6 | residues 29-291 |
| 27 | 290 | 0.98 | 9F0T | His6; Thrombin site; residues 18-293; A18M, F20S, A22S +2 more |
| 25 | 267 | 1.72 | 2GDN | residues 41-307 |
| 21 | 265 | 0.83 | 8RMA | residues 47-311; Y47G, A48P |
| 20 | 263 | 0.88 | 2P74 | residues 29-291 |
| 18 | 265 | 1.05 | 2ZD8 | residues 22-286 |
| 15 | 265 | 1.40 | 3N8L | residues 43-307; E182A |
| 14 | 275 | 1.40 | 9IVL | His6; residues 26-294; H26M, A27G, E170A |
| 11 | 275 | 2.00 | 9UJ6 | His6; residues 26-294; H26M, A27G |
| 10 | 262 | 0.94 | 2ZQ7 | residues 30-291; E169A, R275N, R277N |
| 10 | 263 | 0.85 | 1M40 | residues 24-286; M180T |
| 9 | 290 | 1.25 | 6Z24 | His6; Thrombin site; residues 18-293; A18M, F20S, A22S +3 more |
| 8 | 263 | 1.73 | 1JTG | residues 24-286; V82I, A182V |
| 8 | 265 | 1.30 | 3M6B | residues 43-307 |
| 8 | 291 | 1.70 | 9G7V | matches the canonical sequence |
| 7 | 263 | 1.70 | 1ERM | residues 24-286 |
| 7 | 274 | 1.19 | 5NJ2 | no UniProt reference for this entity, so it cannot be diffed against a canonical sequence |
| 6 | 263 | 1.10 | 4HBT | residues 29-291 |
| 6 | 263 | 1.45 | 3HRE | residues 29-291; S73G |
| 6 | 264 | 1.23 | 3C5A | residues 26-289 |
| 6 | 268 | 1.44 | 6B1F | residues 22-289 |
| 5 | 261 | 1.40 | 7ZPV | residues 31-291 |
| 5 | 263 | 0.85 | 5VLE | residues 29-291; E169A |
| 5 | 265 | 1.65 | 2WK0 | residues 43-307; A75T, A147T, V201A +4 more |
| 5 | 267 | 1.93 | 9W7O | residues 28-294 |
Showing the 25 most-used of 337.
Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".
| Oligomeric state | Chains | Entries | Share |
|---|---|---|---|
| monomeric | 1 | 701 | 91.2% |
| dimeric | 2 | 55 | 7.2% |
| tetrameric | 4 | 11 | 1.4% |
| trimeric | 3 | 2 | 0.3% |
483 entries have the depositor's assembly corroborated by PISA, 270 carry the depositor's word alone and 16 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 12 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 3LEZ, 4EQI, 4IBR, 4OP5, 4OP8, 4OPQ, 4OPR, 4OPZ, 4OQ0, 4OQH, 4OQI, 6MK6.
Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.
| Domain | Source | Span (seed) | Chains |
|---|---|---|---|
| DD-peptidase/beta-lactamase superfamily | CATH 3.40.710.10 | 33–286 | 581 |
| Periplasmic binding protein-like II | CATH 3.40.190.10 | 281–286 | 10 |
| beta-lactamase/transpeptidase-like | SCOP2B 8041576 | 24–286 | 77 |
| beta-lactamase/transpeptidase-like | SCOP2B 8038399 | 25–286 | 43 |
| beta-lactamase/transpeptidase-like | SCOP2B 8069801 | 31–286 | 37 |
| beta-lactamase/transpeptidase-like | SCOP2B 8069815 | 31–286 | 31 |
| beta-lactamase/transpeptidase-like | SCOP2B 8037342 | 31–286 | 16 |
| beta-lactamase/transpeptidase-like | SCOP2B 8069805 | 32–286 | 50 |
| beta-lactamase/transpeptidase-like | SCOP2B 8069809 | 33–286 | 12 |
| beta-lactamase/transpeptidase-like | SCOP2B 8069821 | 34–286 | 18 |
| beta-lactamase/transpeptidase-like | SCOP2B 8069779 | 34–286 | 8 |
| beta-lactamase/transpeptidase-like | SCOP2B 8069823 | 35–286 | 78 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| SO4 | ion | Sulfate Ion | 204 | 0.83 |
| PO4 | ion | Phosphate Ion | 105 | 0.79 |
| GOL | cryoprotectant | Glycerol | 105 | 0.98 |
| CL | ion | Chloride Ion | 81 | 0.83 |
| EDO | cryoprotectant | 1,2-Ethanediol | 63 | 1.08 |
| NA | ion | Sodium Ion | 43 | 0.83 |
| MA4 | ligand | Cyclohexyl-Hexyl-Beta-D-Maltoside | 40 | 0.90 |
| ACT | cryoprotectant | Acetate Ion | 36 | 1.19 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 36 | 1.19 |
| NXL | ligand | (2s,5r)-1-Formyl-5-[(Sulfooxy)amino]piperidine-2-Carboxamide | 36 | 0.83 |
| K | ion | Potassium Ion | 23 | 0.79 |
| EPE | buffer | 4-(2-Hydroxyethyl)-1-Piperazine Ethanesulfonic Acid | 23 | 0.90 |
| PG4 | cryoprotectant | Tetraethylene Glycol | 20 | 1.05 |
| BO4 | ion | Borate Ion | 20 | 1.50 |
| DMS | cryoprotectant | Dimethyl Sulfoxide | 19 | 0.85 |
| CIT | buffer | Citric Acid | 18 | 0.99 |
| CA | ion | Calcium Ion | 18 | 1.05 |
| TSL | ligand | Trans-Enamine Intermediate Of Sulbactam | 13 | 1.30 |
| YCH | ligand | [(4~{S})-2-Oxidanyl-1,3,2-Dioxaborolan-4-Yl]methanol | 12 | 1.00 |
| MES | buffer | 2-(N-Morpholino)-Ethanesulfonic Acid | 11 | 1.05 |
Parsed from the free text 721 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 744
entries that recorded anything at all.
Median pH 7.0
(range 3.4 to 9.5).
769 entries carry a wwPDB validation report: 584 clean, 125 worth a check and 60 with something to explain. Median clashscore 3.81, median RSRZ outliers 1.54%, median R-free minus R-work 0.034. 745 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Escherichia coli | 234 | 0.79 | 118 | 100% |
| Klebsiella pneumoniae | 225 | 0.83 | 163 | 99% |
| Mycobacterium tuberculosis | 66 | 1.19 | 40 | 86% |
| Bacillus licheniformis | 32 | 1.24 | 19 | 87% |
| Serratia marcescens | 31 | 1.40 | 28 | 89% |
| Mycobacterium tuberculosis H37Rv | 20 | 1.40 | 16 | 86% |
| synthetic construct | 19 | 1.30 | 5 | 93% |
| Staphylococcus aureus | 17 | 1.76 | 4 | 90% |
| Pseudomonas aeruginosa | 16 | 0.96 | 5 | 90% |
| Burkholderia thailandensis | 9 | 1.30 | 4 | 86% |
| Klebsiella pneumoniae IS53 | 6 | 0.91 | 0 | 89% |
| Klebsiella pneumoniae subsp. pneumoniae HS11286 | 6 | 1.17 | 3 | 89% |
286 residues, numbered every ten. Every identity figure in this document is measured against this sequence.
active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions
Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.
One record per paper, not per entry.
| Year | Citation |
|---|---|
| 2026 | NCY-1 beta-Lactamase Activity Correlates With Antimicrobial Susceptibility of a Clinical Strain of Nocardia cyriacigeorgica. Microbiologyopen doi:10.1002/mbo3.70267 |
| 2026 | Fused 3D boron heterocycles via EnT catalysis: synthesis, modification and validation as beta-lactamase inhibitors. Chem Sci doi:10.1039/d5sc05518k |
| 2026 | Drop-on-fixed-target reaction initiation approach for serial and time-resolved crystallography. Iucrj doi:10.1107/S2052252526003489 |
| 2026 | Structure-Based Design of Reversible, Quinoline-2(1 H )‐one Inhibitors of Serine- and Metallo-Carbapenemases. Acs Omega doi:10.1021/acsomega.5c12676 |
| 2026 | Beyond structure and activity: targeting class A carbapenemases with monocyclic and bicyclic boronic acids to counter antimicrobial resistance. Org.Biomol.Chem. doi:10.1039/d5ob01703c |
| 2026 | A novel fusion tool to enable G protein-coupled receptor structure determination. Acta Crystallogr D Struct Biol doi:10.1107/S2059798326003785 |
| 2025 | Structural genomics of bacterial drug targets: Application of a high-throughput pipeline to solve 58 protein structures from pathogenic and related bacteria. Microbiol Resour Announc doi:10.1128/mra.00200-25 |
| 2025 | Burkholderia pseudomallei PenI beta-lactamase and variants are potently inhibited by taniborbactam. Antimicrob.Agents Chemother. doi:10.1128/aac.00787-25 |
| 2025 | Directed evolution of a beta-lactamase samples a wide variety of conformational states. Protein Sci. doi:10.1002/pro.70322 |
| 2025 | Phosphate ions modulate enzyme activity and epistatic effects in two clavulanic acid-resistant beta-lactamase mutants. Protein Sci. doi:10.1002/pro.70325 |
| 2025 | Combining MicroED and native mass spectrometry for structural discovery of enzyme-small molecule complexes. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2503780122 |
| 2025 | A beta-lactamase inhibitory protein mutant displays high potency and a broad inhibition profile due to an altered binding mode with beta-lactamases. J.Biol.Chem. doi:10.1016/j.jbc.2025.110850 |
| 2025 | Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography. Nat Commun doi:10.1038/s41467-025-61631-2 |
| 2025 | Binding mode of Isoxazolyl Penicillins to a Class-A beta-lactamase at ambient conditions. Commun Chem doi:10.1038/s42004-025-01801-x |
| 2025 | A glycine at position 105 leads to clavulanic acid and avibactam resistance in class A beta-lactamases. J.Biol.Chem. doi:10.1016/j.jbc.2025.110347 |
| 2025 | Structural Insights into the Role of the Stereochemistry of the Cyclopropyl Ring in the Inhibitory Activity of Xeruborbactam against SME-1 Class A Carbapenemase. Biochemistry doi:10.1021/acs.biochem.5c00336 |
| 2024 | Time-resolved crystallography of boric acid binding to the active site serine of the beta-lactamase CTX-M-14 and subsequent 1,2-diol esterification. Commun Chem doi:10.1038/s42004-024-01236-w |
| 2024 | Crystal structure of the class A extended-spectrum beta-lactamase CTX-M-96 in complex with relebactam at 1.03 Angstrom resolution. Antimicrob.Agents Chemother. doi:10.1128/aac.01721-23 |
| 2024 | Dynamical responses predict a distal site that modulates activity in an antibiotic resistance enzyme. Chem Sci doi:10.1039/d4sc03295k |
| 2024 | Biochemical and structural characterization of a class A beta-lactamase from Nocardia cyriacigeorgica. Acta Crystallogr.,Sect.F doi:10.1107/S2053230X23010671 |
| 2024 | Characterization of the extended substrate spectrum of the class A beta-lactamase CESS-1 from Stenotrophomonas sp. and structure-based investigation into its substrate preference. Int J Antimicrob Agents doi:10.1016/j.ijantimicag.2024.107171 |
| 2024 | Conserved proline residues prevent dimerization and aggregation in the beta-lactamase BlaC. Protein Sci. doi:10.1002/pro.4972 |
| 2024 | A low-barrier proton shared between two aspartates acts as a conformational switch that changes the substrate specificity of the beta-lactamase BlaC. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2024.134665 |
| 2024 | Network of epistatic interactions in an enzyme active site revealed by large-scale deep mutational scanning. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2313513121 |
| 2024 | Restricted Rotational Flexibility of the C5 alpha-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the GES-5 Carbapenemase. Acs Infect Dis. doi:10.1021/acsinfecdis.3c00683 |
| 2024 | Simultaneous enhancement of multiple functional properties using evolution-informed protein design. Nat Commun doi:10.1038/s41467-024-49119-x |
| 2024 | A systematic comparison of Kapton-based HARE chips for fixed-target serial crystallography Cell Rep Phys Sci doi:10.1016/j.xcrp.2024.101987 |
| 2023 | Biochemical and Structural Characterization of CRH-1, a Carbapenemase from Chromobacterium haemolyticum Related to KPC beta-Lactamases. Antimicrob.Agents Chemother. doi:10.1128/aac.00061-23 |
| 2023 | Tautomer-Specific Deacylation and Omega-Loop Flexibility Explain the Carbapenem-Hydrolyzing Broad-Spectrum Activity of the KPC-2 beta-Lactamase. J.Am.Chem.Soc. doi:10.1021/jacs.2c12123 |
| 2023 | Exploring avibactam and relebactam inhibition of Klebsiella pneumoniae carbapenemase D179N variant: role of the Omega loop-held deacylation water. Antimicrob.Agents Chemother. doi:10.1128/aac.00350-23 |
| 2023 | Klebsiella pneumoniae carbapenemase variant 44 acquires ceftazidime-avibactam resistance by altering the conformation of active-site loops. J.Biol.Chem. doi:10.1016/j.jbc.2023.105493 |
| 2023 | Mapping the determinants of catalysis and substrate specificity of the antibiotic resistance enzyme CTX-M beta-lactamase. Commun Biol doi:10.1038/s42003-023-04422-z |
| 2023 | Mutagenesis and structural analysis reveal the CTX-M beta-lactamase active site is optimized for cephalosporin catalysis and drug resistance. J.Biol.Chem. doi:10.1016/j.jbc.2023.104630 |
| 2023 | Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M beta-Lactamases: Biochemical and Structural Analyses. Antimicrob.Agents Chemother. doi:10.1128/aac.00930-22 |
| 2023 | Millisecond cryo-trapping by the spitrobot crystal plunger simplifies time-resolved crystallography. Nat Commun doi:10.1038/s41467-023-37834-w |
| 2023 | Asp179 in the class A beta-lactamase from Mycobacterium tuberculosis is a conserved yet not essential residue due to epistasis. Febs J. doi:10.1111/febs.16892 |
| 2023 | Enhanced activity against a third-generation cephalosporin by destabilization of the active site of a class A beta-lactamase. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2023.126160 |
| 2023 | Heterogeneity in M. tuberculosis beta-lactamase inhibition by Sulbactam. Nat Commun doi:10.1038/s41467-023-41246-1 |
| 2022 | Penicillanic Acid Sulfones Inactivate the Extended-Spectrum beta-Lactamase CTX-M-15 through Formation of a Serine-Lysine Cross-Link: an Alternative Mechanism of beta-Lactamase Inhibition. Mbio doi:10.1128/mbio.01793-21 |
| 2022 | Structural Characterization of the D179N and D179Y Variants of KPC-2 beta-Lactamase: Omega-Loop Destabilization as a Mechanism of Resistance to Ceftazidime-Avibactam. Antimicrob.Agents Chemother. doi:10.1128/aac.02414-21 |