CODSWALLOP

Beta-lactamase inhibitory protein

Streptomyces clavuligerus · seed P35804 · 201 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026

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.

20Entries 20Entities 10Constructs 2Organisms 0Ligand-bound
1.40 ÅBest res.
1.80 ÅMedian res.

Every figure here is counted over the whole family rather than quoted from one entry.

The reference structure

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.

Rendered structure of 3C4P
3C4P at the RCSB · open it in the 3D viewer

Which residues anyone has ever seen

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.

110020120 constructs

Constructs, most-used first

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.

EntitiesLengthBest (Å)Best entryWhat 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

Positions people deliberately mutate

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".

E109W 25% F178L 20% Y87A 15% K110Y 15% S166Y 15% Y179F 15% W186H 15% G38S 10% V39G 10% M40F 10% T41S 10% G42A 10% A43E 10% F45Y 10% T46E 10% R54F 10% Q55D 10% Q56E 10% L58W 10% D59E 10% A61G 10% A63G 10% N65A 10% E67D 10% S71V 10% F72I 10% H77L 10% R79F 10% G80T 10% H81E 10%

What it assembles into

Oligomeric stateChainsEntriesShare
dimeric2 18 90.0%
monomeric1 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.

Domain architecture

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.

CATHDD-peptidase/beta-lactamas3.30.1450.10SCOP2BBLIP repeat-likebeta-lactamase/transpeptidBLIP repeat-like1100201
DomainSourceSpan (seed)Chains
DD-peptidase/beta-lactamase superfamilyCATH 3.40.710.10 37–201 3
3.30.1450.10CATH 111–201 20
BLIP repeat-likeSCOP2B 8041615 37–113 13
beta-lactamase/transpeptidase-likeSCOP2B 8041576 37–201 3
BLIP repeat-likeSCOP2B 8092081 114–201 13

What binds it

ComponentClassNameEntriesBest (Å)
CAion Calcium Ion 3 1.73
SO4ion Sulfate Ion 3 1.70
NH4ion Ammonium Ion 1 1.98
TAMbuffer Tris(Hydroxyethyl)aminomethane 1 1.80
PO4ion Phosphate Ion 1 2.10

How it crystallises

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).

Precipitants

PEG × Sodium chloride × Ammonium sulfate × Dioxane × Sodium citrate × Calcium chloride × Magnesium chloride ×

Buffers

Citrate × Tris × Sodium acetate × Bis-Tris × Sodium cacodylate × Phosphate × MES ×

Which entries to trust

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.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Streptomyces clavuligerus18 1.40 0 82%
Streptomyces exfoliatus2 1.80 0 79%

Seed sequence

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

1MRTVGIGAGV RRLGRAVVMA AAVGGLVLGS AGASNAAGVM TGAKFTQIQF GMTRQQVLDI
61AGAENCETGG SFGDSIHCRG HAAGDYYAYA TFGFTSAAAD AKVDSKSQEK LLAPSAPTLT
121LAKFNQVTVG MTRAQVLATV GQGSCTTWSE YYPAYPSTAG VTLSLSCFDV DGYSSTGFYR
181GSAHLWFTDG VLQGKRQWDL V

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.

Primary citations

One record per paper, not per entry.

YearCitation
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