9CST: Streptavidin-E101Q-K121A

Streptavidin-E101Q-K121A bound to Cu(II)-biotin-ethyl-dipicolylamine cofactor. Determined by X-ray diffraction at 1.13 Å resolution. Released 11 Dec 2024.

Method
X-ray diffraction
Resolution
1.13 Å
Organism
Streptomyces avidinii
Chains
1
Atoms
1,121
Mol. weight
17.23 kDa
Ligands
QG7, CU
Released
11 Dec 2024

Explore 9CST in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CST contains 3 α-helices and 8 β-strands across 1 chain. 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
α-helix14-174
β-strand19-2351
β-strand28-3361
β-strand38-4471
β-strand54-6071
β-strand71-80101
β-strand85-97131
β-strand103-112101
α-helix1131
α-helix116-1216
β-strand123-13191

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
StreptavidinAprotein159Streptomyces avidiniiP22629 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9CST_1 Streptavidin (chains A)
MASMTGGQQMGRDEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRY
DSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGAQARINTQWLLTSGTTEANAW
ASTLVGHDTFTKVKPSAASIDAAKKAGVNNGNPLDAVQQ

Ligands and cofactors

IDNameFormulaCopies
QG7N-(2-{bis[(pyridin-2-yl)methyl]amino}ethyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-t…C24 H32 N6 O2 S1
CUCopper (II) ionCu4

Primary citation

Selective oxidation of active site aromatic residues in engineered Cu proteins. Uyeda, K.S., Follmer, A.H., Borovik, A.S. Chem Sci (2024) 16:98-103. DOI 10.1039/d4sc06667g · 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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