4GDA: Circular Permuted Streptavidin A50/N49

Circular Permuted Streptavidin A50/N49. Determined by X-ray diffraction at 1.0 Å resolution. Released 5 Jun 2013.

Method
X-ray diffraction
Resolution
1.0 Å
Organism
Streptomyces avidinii
Chains
2
Atoms
2,455
Mol. weight
28.18 kDa
Ligands
EOH, BTN
Released
5 Jun 2013

Explore 4GDA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GDA contains 5 α-helices and 16 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand54-6071
β-strand71-80101
β-strand85-97131
β-strand103-112101
α-helix1131
α-helix116-1216
β-strand123-132101
α-helix213-2175
β-strand219-22351
β-strand228-23361
β-strand238-24471
Chain B: 2 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand53-6082
β-strand71-80102
β-strand85-97132
β-strand103-112102
α-helix1131
α-helix116-1216
β-strand123-13192
β-strand219-22352
β-strand228-23362
β-strand238-24472

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
StreptavidinA, Bprotein131Streptomyces avidiniiP22629 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4GDA_1 Streptavidin (chains A, B)
AESRYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWL
LTSGTTEANAWKSTLVGHDTFTKVKPSAASGGGSAEAGITGTWYNQLGSTFIVTAGADGA
LTGTYESAVGN

Ligands and cofactors

IDNameFormulaCopies
EOHEthanolC2 H6 O1
BTNBiotinC10 H16 N2 O3 S2

Water and common crystallization additives (SO4, GOL) are not listed.

Primary citation

Structural consequences of cutting a binding loop: two circularly permuted variants of streptavidin. Le Trong, I., Chu, V., Xing, Y. et al. Acta Crystallogr D Biol Crystallogr (2013) 69:968-977. DOI 10.1107/S0907444913003855 · PubMed

Other PDB entries of the same protein (UniProt P22629 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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