CODSWALLOP

Streptavidin

Streptomyces avidinii · seed P22629 · 183 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.

383Entries 388Entities 164Constructs 12Organisms 259Ligand-bound
0.85 ÅBest res.
1.66 ÅMedian res.

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

The reference structure

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.

Rendered structure of 7ZX9
7ZX9 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.

191183388 constructs

Constructs, most-used first

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.

EntitiesLengthBest (Å)Best entryWhat 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.

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".

A36R 59% A37D 51% E38K 23% K145A 22% S69T 21% S136Y 20% L148R 20% R77N 19% F53M 19% T138V 19% E68T 18% N142D 18% Y46T 17% A141G 17% E75T 17% H151I 17% A62E 17% N73T 17% A39C 17% V79I 16% N129K 16% E140D 16% S146A 16% G58N 16% D60R 16% A110S 16% L97F 16% T115V 16% A102N 16% V121F 16%

What it assembles into

Oligomeric stateChainsEntriesShare
tetrameric4 298 77.8%
octameric8 42 11.0%
dimeric2 25 6.5%
monomeric1 10 2.6%
hexameric6 5 1.3%
heptameric7 2 0.5%
decameric10 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.

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.

CATHAvidin-likeSCOP2BAvidin/streptavidinAvidin/streptavidinAvidin/streptavidinAvidin/streptavidin191183
DomainSourceSpan (seed)Chains
Avidin-likeCATH 2.40.128.30 40–160 266
Avidin/streptavidinSCOP2B 8040372 40–158 287
Avidin/streptavidinSCOP2B 8042736 43–163 24
Avidin/streptavidinSCOP2B 8070804 43–161 4
Avidin/streptavidinSCOP2B 8070814 49–165 5

What binds it

BTN BTN73 entries NAG NAG18 entries IMI IMI9 entries HL9 HL99 entries BNI BNI8 entries KM3 KM38 entries 4IR 4IR7 entries A1BIA A1BIA7 entries LEA LEA6 entries QG7 QG76 entries BTQ BTQ4 entries 0OD 0OD4 entries
ComponentClassNameEntriesBest (Å)
BTNcofactor Biotin 73 0.85
GOLcryoprotectant Glycerol 59 0.85
SO4ion Sulfate Ion 50 1.00
ACTcryoprotectant Acetate Ion 26 1.30
NAGcofactor 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose 18 1.70
CLion Chloride Ion 18 1.30
CUion Copper (Ii) Ion 17 1.13
FMTbuffer Formic Acid 14 1.00
EDOcryoprotectant 1,2-Ethanediol 13 1.00
PEGcryoprotectant Di(Hydroxyethyl)ether 11 1.27
IMIligand 2-Iminobiotin 9 1.30
NAion Sodium Ion 9 1.10
HL9ligand 5-[(3~{A}~{S},4~{S},6~{A}~{R})-2-Oxidanylidene-1,3,3~{A},4,6,6~{ 9 1.00
BNIligand 5-(2-Oxo-Hexahydro-Thieno[3,4-D]imidazol-6-Yl)-Pentanoic Acid (4 8 1.05
KM3ligand {N-(4-{Bis[(Pyridin-2-Yl-Kappan)methyl]amino-Kappan}butyl)-5-[(3 8 1.30
MPDcryoprotectant (4s)-2-Methyl-2,4-Pentanediol 7 0.96
MRDcryoprotectant (4r)-2-Methylpentane-2,4-Diol 7 1.03
4IRligand {N-(4-{(S)-[2-(Amino-Kappan)ethyl]sulfamoyl-Kappan}phenyl)-5-[(3 7 1.60
A1BIAligand N-(3-{Bis[2-(Pyridin-2-Yl)ethyl]amino}propyl)-5-[(3ar,4r,6as)-2- 7 1.40
LEAligand Pentanoic Acid 6 1.45

How it crystallises

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).

Precipitants

Ammonium sulfate × PEG × MPD × Sodium formate × Sodium chloride × Magnesium chloride × Sodium citrate × Lithium sulfate × Isopropanol × Calcium chloride × Tacsimate × PEG (unspecified) × Ammonium phosphate ×

Buffers

Sodium acetate × MES × Bis-Tris × Tris × Citrate × HEPES × Sodium cacodylate × Phosphate × CHES × Imidazole × CAPS × Glycine ×

Which entries to trust

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.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Streptomyces avidinii318 0.85 215 100%
Gallus gallus37 1.00 29 69%
Rhizobium sp. AAP438 1.55 4 52%
Shewanella denitrificans OS2175 1.07 2 61%
Gammaproteobacteria bacterium4 1.67 2 63%
Rhizobium etli CFN 422 1.50 1 63%
Bradyrhizobium japonicum2 1.60 1 63%
Xenopus tropicalis2 1.70 2 64%
Streptomyces sp. H0362 2.03 1 96%
Pleurotus cornucopiae1 1.30 1 72%
Streptomyces1 2.20 0 100%
Danio rerio1 2.40 1 63%

Seed sequence

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

1MRKIVVAAIA VSLTTVSITA SASADPSKDS KAQVSAAEAG ITGTWYNQLG STFIVTAGAD
61GALTGTYESA VGNAESRYVL TGRYDSAPAT DGSGTALGWT VAWKNNYRNA HSATTWSGQY
121VGGAEARINT QWLLTSGTTE ANAWKSTLVG HDTFTKVKPS AASIDAAKKA GVNNGNPLDA
181VQQ

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 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