Streptomyces clavuligerus · seed P35804 · 201 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P35804 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.40.710.10 CATH 3.30.1450.10 SCOP 8041615 SCOP 8041576 SCOP 8092081 RCSB 3C4P 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.
3C4P, 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.
10 distinct constructs across 20 entries. 20 polymer entities differ from the UniProt canonical sequence in some way, 0 carry a recognised expression tag and 0 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 |
|---|---|---|---|---|
| 9 | 165 | 1.40 | 7S5S | residues 37-201 |
| 2 | 156 | 1.80 | 3GMV | residues 31-186 |
| 2 | 165 | 1.65 | 9Q0A | residues 37-201; E109W |
| 1 | 164 | 1.58 | 9Q0B | residues 38-201; E109W |
| 1 | 165 | 1.70 | 3C4O | residues 37-201; E109M, S166K, S182M |
| 1 | 165 | 1.75 | 3C4P | residues 37-201; E109M |
| 1 | 165 | 1.90 | 1XXM | residues 37-201; K110A, F178A, Y179A |
| 1 | 165 | 2.07 | 3C7V | residues 37-201; Y87A |
| 1 | 165 | 2.20 | 3C7U | residues 37-201; W186A |
| 1 | 165 | 2.30 | 1S0W | residues 37-201; F178A |
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 |
|---|---|---|---|
| dimeric | 2 | 18 | 90.0% |
| monomeric | 1 | 2 | 10.0% |
19 entries have the depositor's assembly corroborated by PISA, 1 carry the depositor's word alone and 0 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run.
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 | 37–201 | 3 |
| 3.30.1450.10 | CATH | 111–201 | 20 |
| BLIP repeat-like | SCOP2B 8041615 | 37–113 | 13 |
| beta-lactamase/transpeptidase-like | SCOP2B 8041576 | 37–201 | 3 |
| BLIP repeat-like | SCOP2B 8092081 | 114–201 | 13 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| CA | ion | Calcium Ion | 3 | 1.73 |
| SO4 | ion | Sulfate Ion | 3 | 1.70 |
| NH4 | ion | Ammonium Ion | 1 | 1.98 |
| TAM | buffer | Tris(Hydroxyethyl)aminomethane | 1 | 1.80 |
| PO4 | ion | Phosphate Ion | 1 | 2.10 |
Parsed from the free text 19 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 20
entries that recorded anything at all.
Median pH 6.5
(range 4.2 to 8.8).
20 entries carry a wwPDB validation report: 13 clean, 4 worth a check and 3 with something to explain. Median clashscore 4.62, median RSRZ outliers 3.51%, median R-free minus R-work 0.028. 20 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Streptomyces clavuligerus | 18 | 1.40 | 0 | 82% |
| Streptomyces exfoliatus | 2 | 1.80 | 0 | 79% |
201 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 |
|---|---|
| 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 |
| 2022 | An active site loop toggles between conformations to control antibiotic hydrolysis and inhibition potency for CTX-M beta-lactamase drug-resistance enzymes. Nat Commun doi:10.1038/s41467-022-34564-3 |
| 2011 | Specificity and Cooperativity at beta-lactamase Position 104 in TEM-1/BLIP and SHV-1/BLIP interactions Proteins doi:10.1002/prot.22961 |
| 2009 | Insights into positive and negative requirements for protein-protein interactions by crystallographic analysis of the beta-lactamase inhibitory proteins BLIP, BLIP-I, and BLP. J.Mol.Biol. doi:10.1016/j.jmb.2009.03.058 |
| 2009 | Structural and biochemical characterization of the interaction between KPC-2 beta-lactamase and beta-lactamase inhibitor protein Biochemistry doi:10.1021/bi9007963 |
| 2009 | Structural insight into the kinetics and DeltaCp of interactions between TEM-1 beta-lactamase and beta-lactamase inhibitory protein (BLIP) J.Biol.Chem. doi:10.1074/jbc.M804089200 |
| 2008 | Computational redesign of the SHV-1 beta-lactamase/beta-lactamase inhibitor protein interface. J.Mol.Biol. doi:10.1016/j.jmb.2008.05.051 |
| 2006 | Structural and Computational Characterization of the SHV-1 beta-Lactamase-beta-Lactamase Inhibitor Protein Interface. J.Biol.Chem. doi:10.1074/jbc.M603878200 |
| 2006 | Binding Hot Spots in the TEM1-BLIP Interface in Light of its Modular Architecture. J.Mol.Biol. doi:10.1016/j.jmb.2006.09.076 |
| 2005 | The modular architecture of protein-protein binding interfaces Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.0407280102 |
| 2001 | Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase. Nat.Struct.Biol. doi:10.1038/nsb1001-848 |