Streptomyces avidinii · seed P22629 · 183 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P22629 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 2.40.128.30 SCOP 8040372 SCOP 8042736 SCOP 8070804 SCOP 8070814 RCSB 7ZX9 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.
7ZX9, 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.
164 distinct constructs across 383 entries. 354 polymer entities differ from the UniProt canonical sequence in some way, 10 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 |
|---|---|---|---|---|
| 31 | 123 | 1.30 | 2IZJ | residues 37-159 |
| 23 | 135 | 1.30 | 2RTM | residues 25-159 |
| 18 | 127 | 0.85 | 2F01 | residues 37-163 |
| 15 | 121 | 1.22 | 4Y59 | residues 39-159 |
| 13 | 183 | 1.03 | 5N8B | matches the canonical sequence |
| 10 | 128 | 1.58 | 6XND | residues 25-152; I58T, Q77E |
| 10 | 159 | 1.37 | 5VKX | residues 25-183; D25M, P26A, K28M +8 more |
| 9 | 159 | 1.30 | 6VOZ | residues 25-183; D25M, P26A, K28M +10 more |
| 8 | 121 | 1.46 | 2IZA | residues 37-157 |
| 6 | 153 | 1.40 | 3RDO | His6; residues 18-164; I18M, T19S, A20G +20 more |
| 5 | 129 | 1.40 | 4IRW | residues 35-163; S35G |
| 5 | 159 | 1.31 | 6Y34 | residues 25-183; D25M, P26A, K28M +9 more |
| 5 | 159 | 1.35 | 6UIU | residues 25-183; D25M, P26A, K28M +11 more |
| 5 | 159 | 1.36 | 6AUE | residues 25-183; D25M, P26A, K28M +11 more |
| 4 | 119 | 2.46 | 26CW | residues 40-158 |
| 4 | 159 | 1.40 | 5K68 | residues 25-183; D25M, P26A, K28M +9 more |
| 3 | 120 | 1.20 | 5B5F | residues 40-159 |
| 3 | 122 | 1.07 | 3SZH | residues 41-162; T41M, L42A |
| 3 | 126 | 1.00 | 1Y55 | residues 25-150; C146S |
| 3 | 127 | 1.52 | 6QBB | residues 37-163; A37M, E68V, S69T +4 more |
| 3 | 127 | 1.70 | 1KL3 | residues 37-163; A37M, E68V, S69T +1 more |
| 3 | 127 | 1.70 | 1SWH | residues 37-163; W103F |
| 3 | 128 | 1.89 | 5MYQ | residues 25-152; I58T |
| 3 | 129 | 1.20 | 3WZP | residues 35-163; S35G, A36P, Y46S +7 more |
| 3 | 133 | 1.59 | 4BX6 | residues 37-169; I164E, D165E, A166E +3 more |
Showing the 25 most-used of 164.
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 |
|---|---|---|---|
| tetrameric | 4 | 298 | 77.8% |
| octameric | 8 | 42 | 11.0% |
| dimeric | 2 | 25 | 6.5% |
| monomeric | 1 | 10 | 2.6% |
| hexameric | 6 | 5 | 1.3% |
| heptameric | 7 | 2 | 0.5% |
| decameric | 10 | 1 | 0.3% |
305 entries have the depositor's assembly corroborated by PISA, 69 carry the depositor's word alone and 9 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 32 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1DF8, 1LCV, 1LCZ, 1MM9, 1MOY, 1PTS, 1SRE, 1SRG, 1SRI, 1SWG, 1VWI, 1VWJ, 2IZC, 2IZD, 2IZE, 2RTH, 2RTI, 2RTN, 2RTO, 2RTP.
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 |
|---|---|---|---|
| Avidin-like | CATH 2.40.128.30 | 40–160 | 266 |
| Avidin/streptavidin | SCOP2B 8040372 | 40–158 | 287 |
| Avidin/streptavidin | SCOP2B 8042736 | 43–163 | 24 |
| Avidin/streptavidin | SCOP2B 8070804 | 43–161 | 4 |
| Avidin/streptavidin | SCOP2B 8070814 | 49–165 | 5 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| BTN | cofactor | Biotin | 73 | 0.85 |
| GOL | cryoprotectant | Glycerol | 59 | 0.85 |
| SO4 | ion | Sulfate Ion | 50 | 1.00 |
| ACT | cryoprotectant | Acetate Ion | 26 | 1.30 |
| NAG | cofactor | 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose | 18 | 1.70 |
| CL | ion | Chloride Ion | 18 | 1.30 |
| CU | ion | Copper (Ii) Ion | 17 | 1.13 |
| FMT | buffer | Formic Acid | 14 | 1.00 |
| EDO | cryoprotectant | 1,2-Ethanediol | 13 | 1.00 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 11 | 1.27 |
| IMI | ligand | 2-Iminobiotin | 9 | 1.30 |
| NA | ion | Sodium Ion | 9 | 1.10 |
| HL9 | ligand | 5-[(3~{A}~{S},4~{S},6~{A}~{R})-2-Oxidanylidene-1,3,3~{A},4,6,6~{ | 9 | 1.00 |
| BNI | ligand | 5-(2-Oxo-Hexahydro-Thieno[3,4-D]imidazol-6-Yl)-Pentanoic Acid (4 | 8 | 1.05 |
| KM3 | ligand | {N-(4-{Bis[(Pyridin-2-Yl-Kappan)methyl]amino-Kappan}butyl)-5-[(3 | 8 | 1.30 |
| MPD | cryoprotectant | (4s)-2-Methyl-2,4-Pentanediol | 7 | 0.96 |
| MRD | cryoprotectant | (4r)-2-Methylpentane-2,4-Diol | 7 | 1.03 |
| 4IR | ligand | {N-(4-{(S)-[2-(Amino-Kappan)ethyl]sulfamoyl-Kappan}phenyl)-5-[(3 | 7 | 1.60 |
| A1BIA | ligand | N-(3-{Bis[2-(Pyridin-2-Yl)ethyl]amino}propyl)-5-[(3ar,4r,6as)-2- | 7 | 1.40 |
| LEA | ligand | Pentanoic Acid | 6 | 1.45 |
Parsed from the free text 338 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 352
entries that recorded anything at all.
Median pH 4.5
(range 1.4 to 11.8).
383 entries carry a wwPDB validation report: 92 clean, 178 worth a check and 113 with something to explain. Median clashscore 5.49, median RSRZ outliers 6.45%, median R-free minus R-work 0.035. 353 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Streptomyces avidinii | 318 | 0.85 | 215 | 100% |
| Gallus gallus | 37 | 1.00 | 29 | 69% |
| Rhizobium sp. AAP43 | 8 | 1.55 | 4 | 52% |
| Shewanella denitrificans OS217 | 5 | 1.07 | 2 | 61% |
| Gammaproteobacteria bacterium | 4 | 1.67 | 2 | 63% |
| Rhizobium etli CFN 42 | 2 | 1.50 | 1 | 63% |
| Bradyrhizobium japonicum | 2 | 1.60 | 1 | 63% |
| Xenopus tropicalis | 2 | 1.70 | 2 | 64% |
| Streptomyces sp. H036 | 2 | 2.03 | 1 | 96% |
| Pleurotus cornucopiae | 1 | 1.30 | 1 | 72% |
| Streptomyces | 1 | 2.20 | 0 | 100% |
| Danio rerio | 1 | 2.40 | 1 | 63% |
183 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 | Protein chirality as a determinant of ligand affinity: insights from l- and d-streptavidin. Chem Sci doi:10.1039/d5sc06380a |
| 2025 | Artificial Metalloenzymes with Two Catalytic Cofactors for Tandem Abiotic Transformations. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202422783 |
| 2025 | Biotin/Steptag dual cofactor system for assymetric abiotic transformation in artificial metalloenzymes Nat Synth doi:10.1038/s44160-025-00940-2 |
| 2025 | An Asymmetric Hydrogen Atom Transferase with an Abiological Thiophenol Cofactor. J.Am.Chem.Soc. doi:10.1021/jacs.5c12516 |
| 2025 | Dual-functional co-crystal of streptavidin and ssDNA: electrostatic assembly with positively charged peptide tags. Rsc Adv doi:10.1039/d4ra08326a |
| 2024 | Selective oxidation of active site aromatic residues in engineered Cu proteins. Chem Sci doi:10.1039/d4sc06667g |
| 2024 | Artificial Peroxidase Based on the Biotin-Streptavidin Technology that Rivals the Efficiency of Natural Peroxidases Acs Catalysis doi:10.1021/acscatal.4c03208 |
| 2024 | An artificial nickel chlorinase based on the biotin-streptavidin technology. Chem.Commun.(Camb.) doi:10.1039/d3cc05847f |
| 2024 | An evolved artificial radical cyclase enables the construction of bicyclic terpenoid scaffolds via an H-atom transfer pathway. Nat.Chem. doi:10.1038/s41557-024-01562-5 |
| 2024 | Enantiodivergent synthesis of isoindolones catalysed by a Rh(III)-based artificial metalloenzyme Nat Synth doi:10.1038/s44160-024-00533-5 |
| 2024 | Self-assembled superstructure alleviates air-water interface effect in cryo-EM. Nat Commun doi:10.1038/s41467-024-51696-w |
| 2023 | Self-assembly of a dimeric avidin into unique higher-order oligomers. Febs J. doi:10.1111/febs.16764 |
| 2023 | Manganese Transfer Hydrogenases Based on the Biotin-Streptavidin Technology. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202311896 |
| 2023 | Experimental phasing opportunities for macromolecular crystallography at very long wavelengths. Commun Chem doi:10.1038/s42004-023-01014-0 |
| 2023 | Spiers Memorial Lecture: Shielding the active site: a streptavidin superoxide-dismutase chimera as a host protein for asymmetric transfer hydrogenation. Faraday Disc.Chem.Soc doi:10.1039/d3fd00034f |
| 2023 | The avidin-theophylline complex: A structural and computational study. Proteins doi:10.1002/prot.26538 |
| 2023 | Uniform thin ice on ultraflat graphene for high-resolution cryo-EM. Nat.Methods doi:10.1038/s41592-022-01693-y |
| 2022 | Wilavidin - a novel member of the avidin family that forms unique biotin-binding hexamers. Febs J. doi:10.1111/febs.16259 |
| 2021 | An Artificial Cofactor Catalyzing the Baylis-Hillman Reaction with Designed Streptavidin as Protein Host*. Chembiochem doi:10.1002/cbic.202000880 |
| 2021 | The role of streptavidin and its variants in catalysis by biotinylated secondary amines. Org.Biomol.Chem. doi:10.1039/d1ob01947c |
| 2021 | Artificial Metalloproteins with Dinuclear Iron-Hydroxido Centers. J.Am.Chem.Soc. doi:10.1021/jacs.0c12564 |
| 2021 | Structural Origins of Altered Spectroscopic Properties upon Ligand Binding in Proteins Containing a Fluorescent Noncanonical Amino Acid. Biochemistry doi:10.1021/acs.biochem.1c00291 |
| 2021 | The Role of Changing Loop Conformations in Streptavidin Versions Engineered for High-affinity Binding of the Strep-tag II Peptide. J.Mol.Biol. doi:10.1016/j.jmb.2021.166893 |
| 2021 | Design and evolution of chimeric streptavidin for protein-enabled dual gold catalysis Nat Catal doi:10.1038/s41929-021-00651-9 |
| 2021 | Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites. Iucrj doi:10.1107/S2052252520015675 |
| 2020 | Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity. Sci Rep doi:10.1038/s41598-020-69357-5 |
| 2020 | Enantioselective Hydroxylation of Benzylic C(sp3)-H Bonds by an Artificial Iron Hydroxylase Based on the Biotin-Streptavidin Technology. J.Am.Chem.Soc. doi:10.1021/jacs.0c02788 |
| 2020 | Artificial Iron Proteins: Modeling the Active Sites in Non-Heme Dioxygenases. Inorg.Chem. doi:10.1021/acs.inorgchem.9b03791 |
| 2020 | A Ligand-Directed Nitrophenol Carbonate for Transient in situ Bioconjugation and Drug Delivery Chemmedchem doi:10.1002/cmdc.202000655 |
| 2020 | Genetically fused charged peptides induce rapid crystallization of proteins. Chem.Commun.(Camb.) doi:10.1039/c9cc09529b |
| 2019 | Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source. Acta Crystallogr D Struct Biol doi:10.1107/S2059798319003103 |
| 2019 | Breaking Symmetry: Engineering Single-Chain Dimeric Streptavidin as Host for Artificial Metalloenzymes. J.Am.Chem.Soc. doi:10.1021/jacs.9b06923 |
| 2019 | Single particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution. Nat Commun doi:10.1038/s41467-019-10368-w |
| 2018 | Reactivity and Selectivity of Iminium Organocatalysis Improved by a Protein Host. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.201806850 |
| 2018 | Artificial Metalloproteins Containing Co J. Am. Chem. Soc. doi:10.1021/jacs.7b13052 |
| 2018 | Coordination chemistry within a protein host: regulation of the secondary coordination sphere. Chem. Commun. (Camb.) doi:10.1039/c8cc01931b |
| 2018 | Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coli's Periplasm. J. Am. Chem. Soc. doi:10.1021/jacs.8b07189 |
| 2018 | E. colisurface display of streptavidin for directed evolution of an allylic deallylase. Chem Sci doi:10.1039/c8sc00484f |
| 2018 | Photo-Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin-Streptavidin Technology Helv.Chim.Acta doi:10.1002/hlca.201800036 |
| 2018 | Directed Evolution of an Artificial Imine Reductase. Angew. Chem. Int. Ed. Engl. doi:10.1002/anie.201711016 |